메뉴 건너뛰기




Volumn 7, Issue 1, 2015, Pages 34-68

Rheology of peptide- and protein-based physical hydrogels: Are everyday measurements just scratching the surface?

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MATERIALS; CHARACTERIZATION; CROSSLINKING; FRACTURE; MEDICAL APPLICATIONS; NON NEWTONIAN FLOW; PEPTIDES; RHEOMETERS; SHEAR FLOW; SHEAR THINNING; SHEARING; SHEARING MACHINES; STRESSES; YIELD STRESS;

EID: 84916892201     PISSN: 19395116     EISSN: 19390041     Source Type: Journal    
DOI: 10.1002/wnan.1299     Document Type: Article
Times cited : (114)

References (291)
  • 1
    • 84869231644 scopus 로고    scopus 로고
    • Hydrogels in sensing applications
    • Buenger D, Topuz F, Groll J. Hydrogels in sensing applications. Prog Polym Sci 2012, 37:1678-1719.
    • (2012) Prog Polym Sci , vol.37 , pp. 1678-1719
    • Buenger, D.1    Topuz, F.2    Groll, J.3
  • 3
    • 27644547076 scopus 로고    scopus 로고
    • Development and modeling of electrically triggered hydrogels for microfluidic applications
    • Bassetti MJ, Chatterjee AN, Aluru NR, Beebe DJ. Development and modeling of electrically triggered hydrogels for microfluidic applications. J Microelectromech Syst 2005, 14:1198-1207.
    • (2005) J Microelectromech Syst , vol.14 , pp. 1198-1207
    • Bassetti, M.J.1    Chatterjee, A.N.2    Aluru, N.R.3    Beebe, D.J.4
  • 4
    • 3042635684 scopus 로고    scopus 로고
    • Fabrication of gradient hydrogels using a microfluidics/photopolymerization process
    • Burdick JA, Khademhosseini A, Langer R. Fabrication of gradient hydrogels using a microfluidics/photopolymerization process. Langmuir 2004, 20:5153-5156.
    • (2004) Langmuir , vol.20 , pp. 5153-5156
    • Burdick, J.A.1    Khademhosseini, A.2    Langer, R.3
  • 6
    • 35448983555 scopus 로고    scopus 로고
    • Autonomous microfluidics with stimuli-responsive hydrogels
    • Dong L, Jiang H. Autonomous microfluidics with stimuli-responsive hydrogels. Soft Matter 2007, 3:1223-1230.
    • (2007) Soft Matter , vol.3 , pp. 1223-1230
    • Dong, L.1    Jiang, H.2
  • 7
    • 0037122675 scopus 로고    scopus 로고
    • Hydrogels for biomedical applications
    • Hoffman AS. Hydrogels for biomedical applications. Adv Drug Deliv Rev 2002, 54:3-12.
    • (2002) Adv Drug Deliv Rev , vol.54 , pp. 3-12
    • Hoffman, A.S.1
  • 9
    • 33745135423 scopus 로고    scopus 로고
    • Hydrogels in biology and medicine: from molecular principles to bionanotechnology
    • Peppas NA, Hilt JZ, Khademhosseini A, Langer R. Hydrogels in biology and medicine: from molecular principles to bionanotechnology. Adv Mater 2006, 18:1345-1360.
    • (2006) Adv Mater , vol.18 , pp. 1345-1360
    • Peppas, N.A.1    Hilt, J.Z.2    Khademhosseini, A.3    Langer, R.4
  • 10
    • 0035981078 scopus 로고    scopus 로고
    • Environment-sensitive hydrogels for drug delivery
    • Qiu Y, Park K. Environment-sensitive hydrogels for drug delivery. Adv Drug Deliv Rev 2001, 53:321-339.
    • (2001) Adv Drug Deliv Rev , vol.53 , pp. 321-339
    • Qiu, Y.1    Park, K.2
  • 11
    • 1842484779 scopus 로고    scopus 로고
    • Designing materials for biology and medicine
    • Langer R, Tirrell DA. Designing materials for biology and medicine. Nature 2004, 428:487-492.
    • (2004) Nature , vol.428 , pp. 487-492
    • Langer, R.1    Tirrell, D.A.2
  • 12
    • 0035385135 scopus 로고    scopus 로고
    • Hydrogels for tissue engineering
    • Lee KY, Mooney DJ. Hydrogels for tissue engineering. Chem Rev 2001, 101:1869-1879.
    • (2001) Chem Rev , vol.101 , pp. 1869-1879
    • Lee, K.Y.1    Mooney, D.J.2
  • 13
    • 64249113913 scopus 로고    scopus 로고
    • Photodegradable hydrogels for dynamic tuning of physical and chemical properties
    • Kloxin AM, Kasko AM, Salinas CN, Anseth KS. Photodegradable hydrogels for dynamic tuning of physical and chemical properties. Science 2009, 324:59-63.
    • (2009) Science , vol.324 , pp. 59-63
    • Kloxin, A.M.1    Kasko, A.M.2    Salinas, C.N.3    Anseth, K.S.4
  • 15
    • 70350726217 scopus 로고    scopus 로고
    • Anti-inflammatory peptide-functionalized hydrogels for insulin-secreting cell encapsulation
    • Su J, Hu B-H, Lowe WL Jr, Kaufman DB, Messersmith PB. Anti-inflammatory peptide-functionalized hydrogels for insulin-secreting cell encapsulation. Biomaterials 2010, 31:308-314.
    • (2010) Biomaterials , vol.31 , pp. 308-314
    • Su, J.1    Hu, B.-H.2    Lowe Jr, W.L.3    Kaufman, D.B.4    Messersmith, P.B.5
  • 16
    • 78149264794 scopus 로고    scopus 로고
    • Yielding behavior in injectable hydrogels from telechelic proteins
    • Olsen BD, Kornfield JA, Tirrell DA. Yielding behavior in injectable hydrogels from telechelic proteins. Macromolecules 2010, 43:9094-9099.
    • (2010) Macromolecules , vol.43 , pp. 9094-9099
    • Olsen, B.D.1    Kornfield, J.A.2    Tirrell, D.A.3
  • 17
    • 84859083757 scopus 로고    scopus 로고
    • Improving viability of stem cells during syringe needle flow through the design of hydrogel cell carriers
    • Aguado BA, Mulyasasmita W, Su J, Lampe KJ, Heilshorn SC. Improving viability of stem cells during syringe needle flow through the design of hydrogel cell carriers. Tissue Eng Part A 2012, 18:806-815.
    • (2012) Tissue Eng Part A , vol.18 , pp. 806-815
    • Aguado, B.A.1    Mulyasasmita, W.2    Su, J.3    Lampe, K.J.4    Heilshorn, S.C.5
  • 18
    • 84855731736 scopus 로고    scopus 로고
    • Injectable shear-thinning hydrogels engineered with a self-assembling dock-and-lock mechanism
    • Lu HD, Charati MB, Kim IL, Burdick JA. Injectable shear-thinning hydrogels engineered with a self-assembling dock-and-lock mechanism. Biomaterials 2012, 33:2145-2153.
    • (2012) Biomaterials , vol.33 , pp. 2145-2153
    • Lu, H.D.1    Charati, M.B.2    Kim, I.L.3    Burdick, J.A.4
  • 20
    • 79953871659 scopus 로고    scopus 로고
    • Affinity peptides protect transforming growth factor β during encapsulation in poly(ethylene glycol) hydrogels
    • McCall JD, Lin C-C, Anseth KS. Affinity peptides protect transforming growth factor β during encapsulation in poly(ethylene glycol) hydrogels. Biomacromolecules 2011, 12:1051-1057.
    • (2011) Biomacromolecules , vol.12 , pp. 1051-1057
    • McCall, J.D.1    Lin, C.-C.2    Anseth, K.S.3
  • 21
    • 84855955715 scopus 로고    scopus 로고
    • Tunable growth factor delivery from injectable hydrogels for tissue engineering
    • Vulic K, Shoichet MS. Tunable growth factor delivery from injectable hydrogels for tissue engineering. J Am Chem Soc 2012, 134:882-885.
    • (2012) J Am Chem Soc , vol.134 , pp. 882-885
    • Vulic, K.1    Shoichet, M.S.2
  • 22
    • 7444232477 scopus 로고    scopus 로고
    • DNA delivery from hyaluronic acid-collagen hydrogels via a substrate-mediated approach
    • Segura T, Chung PH, Shea LD. DNA delivery from hyaluronic acid-collagen hydrogels via a substrate-mediated approach. Biomaterials 2005, 26:1575-1584.
    • (2005) Biomaterials , vol.26 , pp. 1575-1584
    • Segura, T.1    Chung, P.H.2    Shea, L.D.3
  • 23
    • 80054685850 scopus 로고    scopus 로고
    • Novel supramolecular gelation route to in situ entrapment and sustained delivery of plasmid DNA
    • Ma D, Zhang H-B, Chen D-H, Zhang L-M. Novel supramolecular gelation route to in situ entrapment and sustained delivery of plasmid DNA. J Colloid Interface Sci 2011, 364:566-573.
    • (2011) J Colloid Interface Sci , vol.364 , pp. 566-573
    • Ma, D.1    Zhang, H.-B.2    Chen, D.-H.3    Zhang, L.-M.4
  • 25
    • 70450191435 scopus 로고    scopus 로고
    • Hydrogel-mediated DNA delivery confers estrogenic response in nonresponsive osteoblast cells
    • Dadsetan M, Szatkowski JP, Shogren KL, Yaszemski MJ, Maran A. Hydrogel-mediated DNA delivery confers estrogenic response in nonresponsive osteoblast cells. J Biomed Mater Res A 2009, 91A:1170-1177.
    • (2009) J Biomed Mater Res A , vol.91 A , pp. 1170-1177
    • Dadsetan, M.1    Szatkowski, J.P.2    Shogren, K.L.3    Yaszemski, M.J.4    Maran, A.5
  • 26
    • 79955866300 scopus 로고    scopus 로고
    • Injectable multidomain peptide nanofiber hydrogel as a delivery agent for stem cell secretome
    • Bakota EL, Wang Y, Danesh FR, Hartgerink JD. Injectable multidomain peptide nanofiber hydrogel as a delivery agent for stem cell secretome. Biomacromolecules 2011, 12:1651-1657.
    • (2011) Biomacromolecules , vol.12 , pp. 1651-1657
    • Bakota, E.L.1    Wang, Y.2    Danesh, F.R.3    Hartgerink, J.D.4
  • 27
    • 78149415045 scopus 로고    scopus 로고
    • The effect of protein structure on their controlled release from an injectable peptide hydrogel
    • Branco MC, Pochan DJ, Wagner NJ, Schneider JP. The effect of protein structure on their controlled release from an injectable peptide hydrogel. Biomaterials 2010, 31:9527-9534.
    • (2010) Biomaterials , vol.31 , pp. 9527-9534
    • Branco, M.C.1    Pochan, D.J.2    Wagner, N.J.3    Schneider, J.P.4
  • 28
    • 69249229499 scopus 로고    scopus 로고
    • Poly(ethylene glycol) hydrogels formed by thiol-ene photopolymerization for enzyme-responsive protein delivery
    • Aimetti AA, Machen AJ, Anseth KS. Poly(ethylene glycol) hydrogels formed by thiol-ene photopolymerization for enzyme-responsive protein delivery. Biomaterials 2009, 30:6048-6054.
    • (2009) Biomaterials , vol.30 , pp. 6048-6054
    • Aimetti, A.A.1    Machen, A.J.2    Anseth, K.S.3
  • 29
    • 58149203184 scopus 로고    scopus 로고
    • Macromolecular diffusion and release from self-assembled β-hairpin peptide hydrogels
    • Branco MC, Pochan DJ, Wagner NJ, Schneider JP. Macromolecular diffusion and release from self-assembled β-hairpin peptide hydrogels. Biomaterials 2009, 30:1339-1347.
    • (2009) Biomaterials , vol.30 , pp. 1339-1347
    • Branco, M.C.1    Pochan, D.J.2    Wagner, N.J.3    Schneider, J.P.4
  • 30
    • 79957921032 scopus 로고    scopus 로고
    • Encapsulation of curcumin in self-assembling peptide hydrogels as injectable drug delivery vehicles
    • Altunbas A, Lee SJ, Rajasekaran SA, Schneider JP, Pochan DJ. Encapsulation of curcumin in self-assembling peptide hydrogels as injectable drug delivery vehicles. Biomaterials 2011, 32:5906-5914.
    • (2011) Biomaterials , vol.32 , pp. 5906-5914
    • Altunbas, A.1    Lee, S.J.2    Rajasekaran, S.A.3    Schneider, J.P.4    Pochan, D.J.5
  • 31
    • 60649096673 scopus 로고    scopus 로고
    • Self-assembling materials for therapeutic delivery
    • Branco MC, Schneider JP. Self-assembling materials for therapeutic delivery. Acta Biomater 2009, 5:817-831.
    • (2009) Acta Biomater , vol.5 , pp. 817-831
    • Branco, M.C.1    Schneider, J.P.2
  • 32
    • 72449205914 scopus 로고    scopus 로고
    • Injectable in situ cross-linking hydrogels for local antifungal therapy
    • Hudson SP, Langer R, Fink GR, Kohane DS. Injectable in situ cross-linking hydrogels for local antifungal therapy. Biomaterials 2010, 31:1444-1452.
    • (2010) Biomaterials , vol.31 , pp. 1444-1452
    • Hudson, S.P.1    Langer, R.2    Fink, G.R.3    Kohane, D.S.4
  • 33
    • 81255158524 scopus 로고    scopus 로고
    • Injectable microgel-hydrogel composites for prolonged small-molecule drug delivery
    • Sivakumaran D, Maitland D, Hoare T. Injectable microgel-hydrogel composites for prolonged small-molecule drug delivery. Biomacromolecules 2011, 12:4112-4120.
    • (2011) Biomacromolecules , vol.12 , pp. 4112-4120
    • Sivakumaran, D.1    Maitland, D.2    Hoare, T.3
  • 35
    • 80052461698 scopus 로고    scopus 로고
    • Injectable block copolymer hydrogels: achievements and future challenges for biomedical applications
    • Cong Truc H, Minh Khanh N, Lee DS. Injectable block copolymer hydrogels: achievements and future challenges for biomedical applications. Macromolecules 2011, 44:6629-6636.
    • (2011) Macromolecules , vol.44 , pp. 6629-6636
    • Cong Truc, H.1    Minh Khanh, N.2    Lee, D.S.3
  • 36
    • 38849102309 scopus 로고    scopus 로고
    • Self-assembly and adhesion of DOPA-modified methacrylic triblock hydrogels
    • Guvendiren M, Messersmith PB, Shull KR. Self-assembly and adhesion of DOPA-modified methacrylic triblock hydrogels. Biomacromolecules 2008, 9:122-128.
    • (2008) Biomacromolecules , vol.9 , pp. 122-128
    • Guvendiren, M.1    Messersmith, P.B.2    Shull, K.R.3
  • 37
    • 70349104175 scopus 로고    scopus 로고
    • Adhesion of DOPA-functionalized model membranes to hard and soft surfaces
    • Guvendiren M, Brass DA, Messersmith PB, Shull KR. Adhesion of DOPA-functionalized model membranes to hard and soft surfaces. J Adhes 2009, 85:631-645.
    • (2009) J Adhes , vol.85 , pp. 631-645
    • Guvendiren, M.1    Brass, D.A.2    Messersmith, P.B.3    Shull, K.R.4
  • 38
    • 70249146893 scopus 로고    scopus 로고
    • Aldehyde-amine chemistry enables modulated biosealants with tissue-specific adhesion
    • Artzi N, Shazly T, Baker AB, Bon A, Edelman ER. Aldehyde-amine chemistry enables modulated biosealants with tissue-specific adhesion. Adv Mater 2009, 21:3399-3403.
    • (2009) Adv Mater , vol.21 , pp. 3399-3403
    • Artzi, N.1    Shazly, T.2    Baker, A.B.3    Bon, A.4    Edelman, E.R.5
  • 41
    • 67849101648 scopus 로고    scopus 로고
    • pH-triggered injectable hydrogels prepared from aqueous N-palmitoyl chitosan: in vitro characteristics and in vivo biocompatibility
    • Chiu YL, Chen SC, Su CJ, Hsiao CW, Chen YM, Chen HL, Sung HW. pH-triggered injectable hydrogels prepared from aqueous N-palmitoyl chitosan: in vitro characteristics and in vivo biocompatibility. Biomaterials 2009, 30:4877-4888.
    • (2009) Biomaterials , vol.30 , pp. 4877-4888
    • Chiu, Y.L.1    Chen, S.C.2    Su, C.J.3    Hsiao, C.W.4    Chen, Y.M.5    Chen, H.L.6    Sung, H.W.7
  • 42
    • 77957712717 scopus 로고    scopus 로고
    • Injectable solid hydrogel: mechanism of shear-thinning and immediate recovery of injectable β-hairpin peptide hydrogels
    • Yan CQ, Altunbas A, Yucel T, Nagarkar RP, Schneider JP, Pochan DJ. Injectable solid hydrogel: mechanism of shear-thinning and immediate recovery of injectable β-hairpin peptide hydrogels. Soft Matter 2010, 6:5143-5156.
    • (2010) Soft Matter , vol.6 , pp. 5143-5156
    • Yan, C.Q.1    Altunbas, A.2    Yucel, T.3    Nagarkar, R.P.4    Schneider, J.P.5    Pochan, D.J.6
  • 43
    • 30744438335 scopus 로고    scopus 로고
    • Electrostatically controlled hydrogelation of oligopeptides and protein entrapment
    • Ramachandran S, Flynn P, Tseng Y, Yu YB. Electrostatically controlled hydrogelation of oligopeptides and protein entrapment. Chem Mater 2005, 17:6583-6588.
    • (2005) Chem Mater , vol.17 , pp. 6583-6588
    • Ramachandran, S.1    Flynn, P.2    Tseng, Y.3    Yu, Y.B.4
  • 44
    • 70349165421 scopus 로고    scopus 로고
    • Self-assembly of multidomain peptides: sequence variation allows control over cross-linking and viscoelasticity
    • Aulisa L, Dong H, Hartgerink JD. Self-assembly of multidomain peptides: sequence variation allows control over cross-linking and viscoelasticity. Biomacromolecules 2009, 10:2694-2698.
    • (2009) Biomacromolecules , vol.10 , pp. 2694-2698
    • Aulisa, L.1    Dong, H.2    Hartgerink, J.D.3
  • 45
  • 46
    • 4744350913 scopus 로고    scopus 로고
    • Salt-triggered peptide folding and consequent self-assembly into hydrogels with tunable modulus
    • Ozbas B, Kretsinger J, Rajagopal K, Schneider JP, Pochan DJ. Salt-triggered peptide folding and consequent self-assembly into hydrogels with tunable modulus. Macromolecules 2004, 37:7331-7337.
    • (2004) Macromolecules , vol.37 , pp. 7331-7337
    • Ozbas, B.1    Kretsinger, J.2    Rajagopal, K.3    Schneider, J.P.4    Pochan, D.J.5
  • 48
    • 84864990683 scopus 로고    scopus 로고
    • Iterative design of peptide-based hydrogels and the effect of network electrostatics on primary chondrocyte behavior
    • Sinthuvanich C, Haines-Butterick LA, Nagy KJ, Schneider JP. Iterative design of peptide-based hydrogels and the effect of network electrostatics on primary chondrocyte behavior. Biomaterials 2012, 33:7478-7488.
    • (2012) Biomaterials , vol.33 , pp. 7478-7488
    • Sinthuvanich, C.1    Haines-Butterick, L.A.2    Nagy, K.J.3    Schneider, J.P.4
  • 49
    • 84856727332 scopus 로고    scopus 로고
    • Evolution-based design of an injectable hydrogel
    • Geisler IM, Schneider JP. Evolution-based design of an injectable hydrogel. Adv Funct Mater 2012, 22:529-537.
    • (2012) Adv Funct Mater , vol.22 , pp. 529-537
    • Geisler, I.M.1    Schneider, J.P.2
  • 50
    • 66149123289 scopus 로고    scopus 로고
    • Folding, self-assembly, and bulk material properties of a De novo designed three-stranded β-sheet hydrogel
    • Rughani RV, Salick DA, Lamm MS, Yucel T, Pochan DJ, Schneider JP. Folding, self-assembly, and bulk material properties of a De novo designed three-stranded β-sheet hydrogel. Biomacromolecules 2009, 10:1295-1304.
    • (2009) Biomacromolecules , vol.10 , pp. 1295-1304
    • Rughani, R.V.1    Salick, D.A.2    Lamm, M.S.3    Yucel, T.4    Pochan, D.J.5    Schneider, J.P.6
  • 51
    • 77957782184 scopus 로고    scopus 로고
    • De novo design of a shear-thin recoverable peptide-based hydrogel capable of intrafibrillar photopolymerization
    • Rughani RV, Branco MC, Pochan D, Schneider JP. De novo design of a shear-thin recoverable peptide-based hydrogel capable of intrafibrillar photopolymerization. Macromolecules 2010, 43:7924-7930.
    • (2010) Macromolecules , vol.43 , pp. 7924-7930
    • Rughani, R.V.1    Branco, M.C.2    Pochan, D.3    Schneider, J.P.4
  • 52
    • 84859571562 scopus 로고    scopus 로고
    • Injectable solid peptide hydrogel as a cell carrier: effects of shear flow on hydrogels and cell payload
    • Yan CQ, Mackay ME, Czymmek K, Nagarkar RP, Schneider JP, Pochan DJ. Injectable solid peptide hydrogel as a cell carrier: effects of shear flow on hydrogels and cell payload. Langmuir 2012, 28:6076-6087.
    • (2012) Langmuir , vol.28 , pp. 6076-6087
    • Yan, C.Q.1    Mackay, M.E.2    Czymmek, K.3    Nagarkar, R.P.4    Schneider, J.P.5    Pochan, D.J.6
  • 53
    • 77955811542 scopus 로고    scopus 로고
    • Rheological properties of peptide-based hydrogels for biomedical and other applications
    • Yan CQ, Pochan DJ. Rheological properties of peptide-based hydrogels for biomedical and other applications. Chem Soc Rev 2010, 39:3528-3540.
    • (2010) Chem Soc Rev , vol.39 , pp. 3528-3540
    • Yan, C.Q.1    Pochan, D.J.2
  • 54
    • 67149107332 scopus 로고    scopus 로고
    • Yield stress fluids slowly yield to analysis
    • Bonn D, Denn MM. Yield stress fluids slowly yield to analysis. Science 2009, 324:1401-1402.
    • (2009) Science , vol.324 , pp. 1401-1402
    • Bonn, D.1    Denn, M.M.2
  • 55
    • 0033079653 scopus 로고    scopus 로고
    • The yield stress - a review or 'pialphanutaualpharhoepsiloniota'-everything flows?
    • Barnes HA. The yield stress - a review or 'pialphanutaualpharhoepsiloniota'-everything flows? J Non-Newton Fluid Mech 1999, 81:133-178.
    • (1999) J Non-Newton Fluid Mech , vol.81 , pp. 133-178
    • Barnes, H.A.1
  • 56
    • 84864538298 scopus 로고    scopus 로고
    • Biological synthesis of circular polypeptides
    • Aboye TL, Camarero JA. Biological synthesis of circular polypeptides. J Biol Chem 2012, 287:27026-27032.
    • (2012) J Biol Chem , vol.287 , pp. 27026-27032
    • Aboye, T.L.1    Camarero, J.A.2
  • 57
    • 0035021281 scopus 로고    scopus 로고
    • Contemporary methods for peptide and protein synthesis
    • Aimoto S. Contemporary methods for peptide and protein synthesis. Curr Org Chem 2001, 5:45-87.
    • (2001) Curr Org Chem , vol.5 , pp. 45-87
    • Aimoto, S.1
  • 58
    • 33748492973 scopus 로고    scopus 로고
    • Synthetic approaches for total chemical synthesis of proteins and protein-like macromolecules of branched architecture
    • Papas S, Strongyis C, Tsikaris V. Synthetic approaches for total chemical synthesis of proteins and protein-like macromolecules of branched architecture. Curr Org Chem 2006, 10:1727-1744.
    • (2006) Curr Org Chem , vol.10 , pp. 1727-1744
    • Papas, S.1    Strongyis, C.2    Tsikaris, V.3
  • 59
    • 67549083305 scopus 로고    scopus 로고
    • Production of self-assembling biomaterials for tissue engineering
    • Kyle S, Aggeli A, Ingham E, McPherson MJ. Production of self-assembling biomaterials for tissue engineering. Trends Biotechnol 2009, 27:423-433.
    • (2009) Trends Biotechnol , vol.27 , pp. 423-433
    • Kyle, S.1    Aggeli, A.2    Ingham, E.3    McPherson, M.J.4
  • 60
    • 70450186565 scopus 로고    scopus 로고
    • Sequence control in polymer synthesis
    • Badi N, Lutz JF. Sequence control in polymer synthesis. Chem Soc Rev 2009, 38:3383-3390.
    • (2009) Chem Soc Rev , vol.38 , pp. 3383-3390
    • Badi, N.1    Lutz, J.F.2
  • 62
    • 79957858634 scopus 로고    scopus 로고
    • Synthetic strategies for the design of peptide/polymer conjugates
    • Dehn S, Chapman R, Jolliffe KA, Perrier S. Synthetic strategies for the design of peptide/polymer conjugates. Polym Rev 2011, 51:214-234.
    • (2011) Polym Rev , vol.51 , pp. 214-234
    • Dehn, S.1    Chapman, R.2    Jolliffe, K.A.3    Perrier, S.4
  • 64
    • 35349019738 scopus 로고    scopus 로고
    • Self-assembly of multidomain peptides: balancing molecular frustration controls conformation and nanostructure
    • Dong H, Paramonov SE, Aulisa L, Bakota EL, Hartgerink JD. Self-assembly of multidomain peptides: balancing molecular frustration controls conformation and nanostructure. J Am Chem Soc 2007, 129:12468-12472.
    • (2007) J Am Chem Soc , vol.129 , pp. 12468-12472
    • Dong, H.1    Paramonov, S.E.2    Aulisa, L.3    Bakota, E.L.4    Hartgerink, J.D.5
  • 66
    • 20144369807 scopus 로고    scopus 로고
    • Repeated rapid shear-responsiveness of peptide hydrogels with tunable shear modulus
    • Ramachandran S, Tseng Y, Yu YB. Repeated rapid shear-responsiveness of peptide hydrogels with tunable shear modulus. Biomacromolecules 2005, 6:1316-1321.
    • (2005) Biomacromolecules , vol.6 , pp. 1316-1321
    • Ramachandran, S.1    Tseng, Y.2    Yu, Y.B.3
  • 67
    • 84884605271 scopus 로고    scopus 로고
    • Salt-induced hydrogels from functionalised-dipeptides
    • Chen L, McDonald TO, Adams DJ. Salt-induced hydrogels from functionalised-dipeptides. RSC Adv 2013, 3:8714-8720.
    • (2013) RSC Adv , vol.3 , pp. 8714-8720
    • Chen, L.1    McDonald, T.O.2    Adams, D.J.3
  • 70
    • 33845968501 scopus 로고    scopus 로고
    • Fracture and adhesion of elastomers and gels: large strains at small length scales
    • Shull KR. Fracture and adhesion of elastomers and gels: large strains at small length scales. J Polym Sci [B] 2006, 44:3436-3439.
    • (2006) J Polym Sci [B] , vol.44 , pp. 3436-3439
    • Shull, K.R.1
  • 71
    • 80053532608 scopus 로고    scopus 로고
    • Structural signature of a brittle-to-ductile transition in self-assembled networks
    • Ramos L, Laperrousaz A, Dieudonne P, Ligoure C. Structural signature of a brittle-to-ductile transition in self-assembled networks. Phys Rev Lett 2011, 107.
    • (2011) Phys Rev Lett , vol.107
    • Ramos, L.1    Laperrousaz, A.2    Dieudonne, P.3    Ligoure, C.4
  • 72
    • 84873523983 scopus 로고    scopus 로고
    • Fractures in complex fluids: the case of transient networks
    • Ligoure C, Mora S. Fractures in complex fluids: the case of transient networks. Rheol Acta 2013, 52:91-114.
    • (2013) Rheol Acta , vol.52 , pp. 91-114
    • Ligoure, C.1    Mora, S.2
  • 73
    • 77952198048 scopus 로고    scopus 로고
    • Strain stiffening in synthetic and biopolymer networks
    • Erk KA, Henderson KJ, Shull KR. Strain stiffening in synthetic and biopolymer networks. Biomacromolecules 2010, 11:1358-1363.
    • (2010) Biomacromolecules , vol.11 , pp. 1358-1363
    • Erk, K.A.1    Henderson, K.J.2    Shull, K.R.3
  • 74
    • 84867888923 scopus 로고    scopus 로고
    • Strain stiffening in collagen I networks
    • Motte S, Kaufman LJ. Strain stiffening in collagen I networks. Biopolymers 2013, 99:35-46.
    • (2013) Biopolymers , vol.99 , pp. 35-46
    • Motte, S.1    Kaufman, L.J.2
  • 75
    • 84867479720 scopus 로고    scopus 로고
    • Natural stiffening increases flaw tolerance of biological fibers
    • Giesa T, Pugno NM, Buehler MJ. Natural stiffening increases flaw tolerance of biological fibers. Phys Rev E 2012, 86.
    • (2012) Phys Rev E , vol.86
    • Giesa, T.1    Pugno, N.M.2    Buehler, M.J.3
  • 76
    • 84858146347 scopus 로고    scopus 로고
    • Early stiffening and softening of collagen: interplay of deformation mechanisms in biopolymer networks
    • Kurniawan NA, Wong LH, Rajagopalan R. Early stiffening and softening of collagen: interplay of deformation mechanisms in biopolymer networks. Biomacromolecules 2012, 13:691-698.
    • (2012) Biomacromolecules , vol.13 , pp. 691-698
    • Kurniawan, N.A.1    Wong, L.H.2    Rajagopalan, R.3
  • 77
    • 41549099586 scopus 로고    scopus 로고
    • Perspectives on shear banding in complex fluids
    • Olmsted PD. Perspectives on shear banding in complex fluids. Rheol Acta 2008, 47:283-300.
    • (2008) Rheol Acta , vol.47 , pp. 283-300
    • Olmsted, P.D.1
  • 80
    • 0032319131 scopus 로고    scopus 로고
    • Rheological characterisation of polymer gels
    • Kavanagh GM, Ross-Murphy SB. Rheological characterisation of polymer gels. Prog Polym Sci 1998, 23:533-562.
    • (1998) Prog Polym Sci , vol.23 , pp. 533-562
    • Kavanagh, G.M.1    Ross-Murphy, S.B.2
  • 82
    • 0030262518 scopus 로고    scopus 로고
    • Relaxation patterns of nearly critical gels
    • Mours M, Winter HH. Relaxation patterns of nearly critical gels. Macromolecules 1996, 29:7221-7229.
    • (1996) Macromolecules , vol.29 , pp. 7221-7229
    • Mours, M.1    Winter, H.H.2
  • 84
    • 0010275044 scopus 로고    scopus 로고
    • Rheology of polymers near solid liquid transition
    • Berlin: Springer Verlag; .
    • Winter HH, Mours M. Rheology of polymers near solid liquid transition. In: Advances in Polymer Science, vol. 134. Berlin: Springer Verlag; 1997.
    • (1997) Advances in Polymer Science , vol.134
    • Winter, H.H.1    Mours, M.2
  • 85
    • 37249063696 scopus 로고    scopus 로고
    • Microrheology: a review of the method and applications
    • Cicuta P, Donald AM. Microrheology: a review of the method and applications. Soft Matter 2007, 3:1449-1455.
    • (2007) Soft Matter , vol.3 , pp. 1449-1455
    • Cicuta, P.1    Donald, A.M.2
  • 87
    • 15544368498 scopus 로고    scopus 로고
    • Microrheology of complex fluids
    • Waigh TA. Microrheology of complex fluids. Rep Prog Phys 2005, 68:685-742.
    • (2005) Rep Prog Phys , vol.68 , pp. 685-742
    • Waigh, T.A.1
  • 88
    • 84864526929 scopus 로고    scopus 로고
    • Microrheology of biomaterial hydrogelators
    • Schultz KM, Furst EM. Microrheology of biomaterial hydrogelators. Soft Matter 2012, 8:6198-6205.
    • (2012) Soft Matter , vol.8 , pp. 6198-6205
    • Schultz, K.M.1    Furst, E.M.2
  • 91
    • 84878450880 scopus 로고    scopus 로고
    • Oscillatory shear rheology for probing nonlinear viscoelasticity of complex fluids: large amplitude oscillatory shear
    • In: Krishnan JM, Deshpande AP, Kumar PBS, eds. . New York: Springer;
    • Deshpande A. Oscillatory shear rheology for probing nonlinear viscoelasticity of complex fluids: large amplitude oscillatory shear. In: Krishnan JM, Deshpande AP, Kumar PBS, eds. Rheology of Complex Fluids. New York: Springer; 2010, 87-110.
    • (2010) Rheology of Complex Fluids , pp. 87-110
    • Deshpande, A.1
  • 93
    • 84878655155 scopus 로고    scopus 로고
    • The importance of the self-assembly process to control mechanical properties of low molecular weight hydrogels
    • Raeburn J, Cardoso AZ, Adams DJ. The importance of the self-assembly process to control mechanical properties of low molecular weight hydrogels. Chem Soc Rev 2013, 42:5143-5156.
    • (2013) Chem Soc Rev , vol.42 , pp. 5143-5156
    • Raeburn, J.1    Cardoso, A.Z.2    Adams, D.J.3
  • 95
    • 77953301141 scopus 로고    scopus 로고
    • Energy transfer in self-assembled dipeptide hydrogels
    • Chen L, Revel S, Morris K, Adams DJ. Energy transfer in self-assembled dipeptide hydrogels. Chem Commun 2010, 46:4267-4269.
    • (2010) Chem Commun , vol.46 , pp. 4267-4269
    • Chen, L.1    Revel, S.2    Morris, K.3    Adams, D.J.4
  • 96
    • 84855379206 scopus 로고    scopus 로고
    • Heavy metal ion hydrogelation of a self-assembling peptide via cysteinyl chelation
    • Knerr PJ, Branco MC, Nagarkar R, Pochan DJ, Schneider JP. Heavy metal ion hydrogelation of a self-assembling peptide via cysteinyl chelation. J Mater Chem 2012, 22:1352-1357.
    • (2012) J Mater Chem , vol.22 , pp. 1352-1357
    • Knerr, P.J.1    Branco, M.C.2    Nagarkar, R.3    Pochan, D.J.4    Schneider, J.P.5
  • 97
    • 31944435655 scopus 로고    scopus 로고
    • Enzyme-triggered self-assembly of peptide hydrogels via reversed hydrolysis
    • Toledano S, Williams RJ, Jayawarna V, Ulijn RV. Enzyme-triggered self-assembly of peptide hydrogels via reversed hydrolysis. J Am Chem Soc 2006, 128:1070-1071.
    • (2006) J Am Chem Soc , vol.128 , pp. 1070-1071
    • Toledano, S.1    Williams, R.J.2    Jayawarna, V.3    Ulijn, R.V.4
  • 100
    • 33644885444 scopus 로고    scopus 로고
    • Intermolecular forces in the self-assembly of peptide amphiphile nanofibers
    • Stendahl JC, Rao MS, Guler MO, Stupp SI. Intermolecular forces in the self-assembly of peptide amphiphile nanofibers. Adv Funct Mater 2006, 16:499-508.
    • (2006) Adv Funct Mater , vol.16 , pp. 499-508
    • Stendahl, J.C.1    Rao, M.S.2    Guler, M.O.3    Stupp, S.I.4
  • 101
    • 28844449157 scopus 로고    scopus 로고
    • Light-activated hydrogel formation via the triggered folding and self-assembly of a designed peptide
    • Haines LA, Rajagopal K, Ozbas B, Salick DA, Pochan DJ, Schneider JP. Light-activated hydrogel formation via the triggered folding and self-assembly of a designed peptide. J Am Chem Soc 2005, 127:17025-17029.
    • (2005) J Am Chem Soc , vol.127 , pp. 17025-17029
    • Haines, L.A.1    Rajagopal, K.2    Ozbas, B.3    Salick, D.A.4    Pochan, D.J.5    Schneider, J.P.6
  • 102
    • 67649433434 scopus 로고    scopus 로고
    • Stem cell- and scaffold-based tissue engineering approaches to osteochondral regenerative medicine
    • Sundelacruz S, Kaplan DL. Stem cell- and scaffold-based tissue engineering approaches to osteochondral regenerative medicine. Semin Cell Dev Biol 2009, 20:646-655.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 646-655
    • Sundelacruz, S.1    Kaplan, D.L.2
  • 103
    • 76949107913 scopus 로고    scopus 로고
    • Responsive and in situ-forming chitosan scaffolds for bone tissue engineering applications: an overview of the last decade
    • Martins AM, Alves CM, Kasper FK, Mikos AG, Reis RL. Responsive and in situ-forming chitosan scaffolds for bone tissue engineering applications: an overview of the last decade. J Mater Chem 2010, 20:1638-1645.
    • (2010) J Mater Chem , vol.20 , pp. 1638-1645
    • Martins, A.M.1    Alves, C.M.2    Kasper, F.K.3    Mikos, A.G.4    Reis, R.L.5
  • 105
    • 27944497333 scopus 로고    scopus 로고
    • Tissue cells feel and respond to the stiffness of their substrate
    • Discher DE, Janmey P, Wang YL. Tissue cells feel and respond to the stiffness of their substrate. Science 2005, 310:1139-1143.
    • (2005) Science , vol.310 , pp. 1139-1143
    • Discher, D.E.1    Janmey, P.2    Wang, Y.L.3
  • 106
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • Engler AJ, Sen S, Sweeney HL, Discher DE. Matrix elasticity directs stem cell lineage specification. Cell 2006, 126:677-689.
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 107
    • 84878106240 scopus 로고    scopus 로고
    • The use of the mechanical microenvironment of phospholipid polymer hydrogels to control cell behavior
    • Oda H, Konno T, Ishihara K. The use of the mechanical microenvironment of phospholipid polymer hydrogels to control cell behavior. Biomaterials 2013, 34:5891-5896.
    • (2013) Biomaterials , vol.34 , pp. 5891-5896
    • Oda, H.1    Konno, T.2    Ishihara, K.3
  • 108
    • 0031671026 scopus 로고    scopus 로고
    • Forces on adhesive contacts affect cell function
    • Galbraith CG, Sheetz MP. Forces on adhesive contacts affect cell function. Curr Opin Cell Biol 1998, 10:566-571.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 566-571
    • Galbraith, C.G.1    Sheetz, M.P.2
  • 112
    • 0023824773 scopus 로고
    • Wall slip corrections for Couette and parallel disk viscometers
    • Yoshimura A, Prudhomme RK. Wall slip corrections for Couette and parallel disk viscometers. J Rheol 1988, 32:53-67.
    • (1988) J Rheol , vol.32 , pp. 53-67
    • Yoshimura, A.1    Prudhomme, R.K.2
  • 113
    • 84879517748 scopus 로고    scopus 로고
    • On the use of rough geometries in rheometry
    • Carotenuto C, Minale M. On the use of rough geometries in rheometry. J Non-Newton Fluid Mech 2013, 198:39-47.
    • (2013) J Non-Newton Fluid Mech , vol.198 , pp. 39-47
    • Carotenuto, C.1    Minale, M.2
  • 114
    • 0041695635 scopus 로고    scopus 로고
    • Yield stress and wall slip phenomena in colloidal silica gels
    • 1978-present)
    • Walls HJ, Caines SB, Sanchez AM, Khan SA. Yield stress and wall slip phenomena in colloidal silica gels. J Rheol (1978-present) 2003, 47:847-868.
    • (2003) J Rheol , vol.47 , pp. 847-868
    • Walls, H.J.1    Caines, S.B.2    Sanchez, A.M.3    Khan, S.A.4
  • 115
    • 84867863760 scopus 로고    scopus 로고
    • Determining the true slip of a yield stress material with a sliding plate rheometer
    • Clasen C. Determining the true slip of a yield stress material with a sliding plate rheometer. Rheologica Acta 2012, 51:883-890.
    • (2012) Rheologica Acta , vol.51 , pp. 883-890
    • Clasen, C.1
  • 116
    • 77957656707 scopus 로고    scopus 로고
    • Wall slip phenomenon assessment of yield stress pseudoplastic fluids in Couette geometry
    • Kelessidis VC, Hatzistamou V, Maglione R. Wall slip phenomenon assessment of yield stress pseudoplastic fluids in Couette geometry. Appl Rheol 2010, 20:U29-U36.
    • (2010) Appl Rheol , vol.20 , pp. U29-U36
    • Kelessidis, V.C.1    Hatzistamou, V.2    Maglione, R.3
  • 117
    • 42749104107 scopus 로고    scopus 로고
    • Semiflexible chain networks formed via self-assembly of β-hairpin molecules
    • Ozbas B, Rajagopal K, Schneider JP, Pochan DJ. Semiflexible chain networks formed via self-assembly of β-hairpin molecules. Phys Rev Lett 2004, 93.
    • (2004) Phys Rev Lett , vol.93
    • Ozbas, B.1    Rajagopal, K.2    Schneider, J.P.3    Pochan, D.J.4
  • 118
    • 29944436353 scopus 로고    scopus 로고
    • Probing the importance of lateral hydrophobic association in self-assembling peptide hydrogelators
    • Rajagopal K, Ozbas B, Pochan DJ, Schneider JP. Probing the importance of lateral hydrophobic association in self-assembling peptide hydrogelators. Europ Biophys J Biophys Lett 2006, 35:162-169.
    • (2006) Europ Biophys J Biophys Lett , vol.35 , pp. 162-169
    • Rajagopal, K.1    Ozbas, B.2    Pochan, D.J.3    Schneider, J.P.4
  • 119
    • 0141596163 scopus 로고    scopus 로고
    • Thermally reversible hydrogels via intramolecular folding and consequent self-assembly of a de Novo designed peptide
    • Pochan DJ, Schneider JP, Kretsinger J, Ozbas B, Rajagopal K, Haines L. Thermally reversible hydrogels via intramolecular folding and consequent self-assembly of a de Novo designed peptide. J Am Chem Soc 2003, 125:11802-11803.
    • (2003) J Am Chem Soc , vol.125 , pp. 11802-11803
    • Pochan, D.J.1    Schneider, J.P.2    Kretsinger, J.3    Ozbas, B.4    Rajagopal, K.5    Haines, L.6
  • 120
    • 50249087525 scopus 로고    scopus 로고
    • Direct observation of early-time hydrogelation in β-hairpin peptide self-assembly
    • Yucel T, Micklitsch CM, Schneider JP, Pochan DJ. Direct observation of early-time hydrogelation in β-hairpin peptide self-assembly. Macromolecules 2008, 41:5763-5772.
    • (2008) Macromolecules , vol.41 , pp. 5763-5772
    • Yucel, T.1    Micklitsch, C.M.2    Schneider, J.P.3    Pochan, D.J.4
  • 121
    • 70349173315 scopus 로고    scopus 로고
    • Tuning the pH responsiveness of β-hairpin peptide folding, self-assembly, and hydrogel material formation
    • Rajagopal K, Lamm MS, Haines-Butterick LA, Pochan DJ, Schneider JP. Tuning the pH responsiveness of β-hairpin peptide folding, self-assembly, and hydrogel material formation. Biomacromolecules 2009, 10:2619-2625.
    • (2009) Biomacromolecules , vol.10 , pp. 2619-2625
    • Rajagopal, K.1    Lamm, M.S.2    Haines-Butterick, L.A.3    Pochan, D.J.4    Schneider, J.P.5
  • 122
    • 49349105563 scopus 로고    scopus 로고
    • In vitro assessment of the pro-inflammatory potential of β-hairpin peptide hydrogels
    • Haines-Butterick LA, Salick DA, Pochan DJ, Schneider JP. In vitro assessment of the pro-inflammatory potential of β-hairpin peptide hydrogels. Biomaterials 2008, 29:4164-4169.
    • (2008) Biomaterials , vol.29 , pp. 4164-4169
    • Haines-Butterick, L.A.1    Salick, D.A.2    Pochan, D.J.3    Schneider, J.P.4
  • 123
    • 70349292650 scopus 로고    scopus 로고
    • Controlling hydrogelation kinetics via peptide design for three-dimensional encapsulation and injectable delivery of cells
    • Haines-Butterick LA, Rajagopal K, Lamm M, Pochan DJ, Schnieder JP. Controlling hydrogelation kinetics via peptide design for three-dimensional encapsulation and injectable delivery of cells. Biopolymers 2007, 88:518.
    • (2007) Biopolymers , vol.88 , pp. 518
    • Haines-Butterick, L.A.1    Rajagopal, K.2    Lamm, M.3    Pochan, D.J.4    Schnieder, J.P.5
  • 125
  • 127
    • 36749074939 scopus 로고    scopus 로고
    • Inherent antibacterial activity of a peptide-based β-hairpin hydrogel
    • Salick DA, Kretsinger JK, Pochan DJ, Schneider JP. Inherent antibacterial activity of a peptide-based β-hairpin hydrogel. J Am Chem Soc 2007, 129:14793-14799.
    • (2007) J Am Chem Soc , vol.129 , pp. 14793-14799
    • Salick, D.A.1    Kretsinger, J.K.2    Pochan, D.J.3    Schneider, J.P.4
  • 128
  • 129
    • 84977820715 scopus 로고    scopus 로고
    • Strand swapping controls the nanostructure of β-hairpin peptide hydrogels
    • Nagarkar RP, Hule RA, Pochan DJ, Schneider JP. Strand swapping controls the nanostructure of β-hairpin peptide hydrogels. Biopolymers 2007, 88:614.
    • (2007) Biopolymers , vol.88 , pp. 614
    • Nagarkar, R.P.1    Hule, R.A.2    Pochan, D.J.3    Schneider, J.P.4
  • 130
    • 70349897841 scopus 로고    scopus 로고
    • Dependence of self-assembled peptide hydrogel network structure on local fibril nanostructure
    • Hule RA, Nagarkar RP, Hammouda B, Schneider JP, Pochan DJ. Dependence of self-assembled peptide hydrogel network structure on local fibril nanostructure. Macromolecules 2009, 42:7137-7145.
    • (2009) Macromolecules , vol.42 , pp. 7137-7145
    • Hule, R.A.1    Nagarkar, R.P.2    Hammouda, B.3    Schneider, J.P.4    Pochan, D.J.5
  • 132
    • 79960080932 scopus 로고    scopus 로고
    • Controlled biodegradation of self-assembling β-hairpin peptide hydrogels by proteolysis with matrix metalloproteinase-13
    • Giano MC, Pochan DJ, Schneider JP. Controlled biodegradation of self-assembling β-hairpin peptide hydrogels by proteolysis with matrix metalloproteinase-13. Biomaterials 2011, 32:6471-6477.
    • (2011) Biomaterials , vol.32 , pp. 6471-6477
    • Giano, M.C.1    Pochan, D.J.2    Schneider, J.P.3
  • 133
    • 80053085593 scopus 로고    scopus 로고
    • Enhanced mechanical rigidity of hydrogels formed from enantiomeric peptide assemblies
    • Nagy KJ, Giano MC, Jin A, Pochan DJ, Schneider JP. Enhanced mechanical rigidity of hydrogels formed from enantiomeric peptide assemblies. J Am Chem Soc 2011, 133:14975-14977.
    • (2011) J Am Chem Soc , vol.133 , pp. 14975-14977
    • Nagy, K.J.1    Giano, M.C.2    Jin, A.3    Pochan, D.J.4    Schneider, J.P.5
  • 135
    • 80052423675 scopus 로고    scopus 로고
    • Rheo-small-angle neutron scattering at the National Institute of Standards and Technology Center for Neutron Research
    • Porcar L, Pozzo D, Langenbucher G, Moyer J, Butler PD. Rheo-small-angle neutron scattering at the National Institute of Standards and Technology Center for Neutron Research. Rev Sci Instrum 2011, 82:083902-1-083902-7.
    • (2011) Rev Sci Instrum , vol.82 , pp. 0839021-0839027
    • Porcar, L.1    Pozzo, D.2    Langenbucher, G.3    Moyer, J.4    Butler, P.D.5
  • 136
    • 84879960273 scopus 로고    scopus 로고
    • Development of a confocal rheometer for soft and biological materials
    • Dutta SK, Mbi A, Arevalo RC, Blair DL. Development of a confocal rheometer for soft and biological materials. Rev Sci Instrum 2013, 84:013709-1-013709-9.
    • (2013) Rev Sci Instrum , vol.84 , pp. 0137091-0137099
    • Dutta, S.K.1    Mbi, A.2    Arevalo, R.C.3    Blair, D.L.4
  • 137
    • 24144457766 scopus 로고    scopus 로고
    • Twenty years of particle image velocimetry
    • Adrian RJ. Twenty years of particle image velocimetry. Exp Fluids 2005, 39:159-169.
    • (2005) Exp Fluids , vol.39 , pp. 159-169
    • Adrian, R.J.1
  • 138
    • 0000839042 scopus 로고    scopus 로고
    • A hybrid digital particle tracking velocimetry technique
    • Cowen EA, Monismith SG. A hybrid digital particle tracking velocimetry technique. Exp Fluids 1997, 22:199-211.
    • (1997) Exp Fluids , vol.22 , pp. 199-211
    • Cowen, E.A.1    Monismith, S.G.2
  • 139
    • 34250073994 scopus 로고
    • Particle tracking velocimetry in 3-dimensional flows .1. photogrammetric determination of particle coordinates
    • Maas HG, Gruen A, Papantoniou D. Particle tracking velocimetry in 3-dimensional flows .1. photogrammetric determination of particle coordinates. Exp Fluids 1993, 15:133-146.
    • (1993) Exp Fluids , vol.15 , pp. 133-146
    • Maas, H.G.1    Gruen, A.2    Papantoniou, D.3
  • 140
    • 0031341825 scopus 로고    scopus 로고
    • Tracer particles and seeding for particle image velocimetry
    • Melling A. Tracer particles and seeding for particle image velocimetry. Meas Sci Technol 1997, 8:1406-1416.
    • (1997) Meas Sci Technol , vol.8 , pp. 1406-1416
    • Melling, A.1
  • 141
    • 42449111638 scopus 로고    scopus 로고
    • Observations of wall slip and shear banding in an entangled DNA solution
    • Boukany PE, Hu YT, Wang SQ. Observations of wall slip and shear banding in an entangled DNA solution. Macromolecules 2008, 41:2644-2650.
    • (2008) Macromolecules , vol.41 , pp. 2644-2650
    • Boukany, P.E.1    Hu, Y.T.2    Wang, S.Q.3
  • 142
    • 60049083516 scopus 로고    scopus 로고
    • Exploring the transition from wall slip to bulk shearing banding in well-entangled DNA solutions
    • Boukany PE, Wang SQ. Exploring the transition from wall slip to bulk shearing banding in well-entangled DNA solutions. Soft Matter 2009, 5:780-789.
    • (2009) Soft Matter , vol.5 , pp. 780-789
    • Boukany, P.E.1    Wang, S.Q.2
  • 143
    • 58149233758 scopus 로고    scopus 로고
    • Shear banding or not in entangled DNA solutions depending on the level of entanglement
    • Boukany PE, Wang SQ. Shear banding or not in entangled DNA solutions depending on the level of entanglement. J Rheol 2009, 53:73-83.
    • (2009) J Rheol , vol.53 , pp. 73-83
    • Boukany, P.E.1    Wang, S.Q.2
  • 144
    • 78149469716 scopus 로고    scopus 로고
    • Flow pattern and molecular visualization of DNA solutions through a 4:1 planar micro-contraction
    • Hemminger OL, Boukany PE, Wang SQ, Lee LJ. Flow pattern and molecular visualization of DNA solutions through a 4:1 planar micro-contraction. J Non-Newton Fluid Mech 2010, 165:1613-1624.
    • (2010) J Non-Newton Fluid Mech , vol.165 , pp. 1613-1624
    • Hemminger, O.L.1    Boukany, P.E.2    Wang, S.Q.3    Lee, L.J.4
  • 146
    • 40549106842 scopus 로고    scopus 로고
    • Use of particle-tracking velocimetry and flow birefringence to study nonlinear flow behavior of entangled wormlike micellar solution: from wall slip, bulk disentanglement to chain scission
    • Boukany PE, Wang SQ. Use of particle-tracking velocimetry and flow birefringence to study nonlinear flow behavior of entangled wormlike micellar solution: from wall slip, bulk disentanglement to chain scission. Macromolecules 2008, 41:1455-1464.
    • (2008) Macromolecules , vol.41 , pp. 1455-1464
    • Boukany, P.E.1    Wang, S.Q.2
  • 148
    • 78751490068 scopus 로고    scopus 로고
    • Homogeneous shear, wall slip, and shear banding of entangled polymeric liquids in simple-shear rheometry: a roadmap of nonlinear rheology
    • Wang SQ, Ravindranath S, Boukany PE. Homogeneous shear, wall slip, and shear banding of entangled polymeric liquids in simple-shear rheometry: a roadmap of nonlinear rheology. Macromolecules 2011, 44:183-190.
    • (2011) Macromolecules , vol.44 , pp. 183-190
    • Wang, S.Q.1    Ravindranath, S.2    Boukany, P.E.3
  • 149
    • 77953298168 scopus 로고    scopus 로고
    • Transition from "brittle" to "ductile" rheological behavior by tuning the morphology of self-assembled networks
    • Tixier T, Tabuteau H, Carriere A, Ramos L, Ligoure C. Transition from "brittle" to "ductile" rheological behavior by tuning the morphology of self-assembled networks. Soft Matter 2010, 6:2699-2707.
    • (2010) Soft Matter , vol.6 , pp. 2699-2707
    • Tixier, T.1    Tabuteau, H.2    Carriere, A.3    Ramos, L.4    Ligoure, C.5
  • 150
    • 17744406060 scopus 로고    scopus 로고
    • Evidence of shear-induced fluid fracture in telechelic polymer networks
    • Berret JF, Serero Y. Evidence of shear-induced fluid fracture in telechelic polymer networks. Phys Rev Lett 2001, 87.
    • (2001) Phys Rev Lett , vol.87
    • Berret, J.F.1    Serero, Y.2
  • 153
    • 68949090079 scopus 로고    scopus 로고
    • The effect of increasing hydrophobicity on the self-assembly of amphipathic β-sheet peptides
    • Bowerman CJ, Ryan DM, Nissan DA, Nilsson BL. The effect of increasing hydrophobicity on the self-assembly of amphipathic β-sheet peptides. Mol Biosyst 2009, 5:1058-1069.
    • (2009) Mol Biosyst , vol.5 , pp. 1058-1069
    • Bowerman, C.J.1    Ryan, D.M.2    Nissan, D.A.3    Nilsson, B.L.4
  • 154
    • 77954645079 scopus 로고    scopus 로고
    • A reductive trigger for peptide self-assembly and hydrogelation
    • Bowerman CJ, Nilsson BL. A reductive trigger for peptide self-assembly and hydrogelation. J Am Chem Soc 2010, 132:9526-9527.
    • (2010) J Am Chem Soc , vol.132 , pp. 9526-9527
    • Bowerman, C.J.1    Nilsson, B.L.2
  • 155
    • 33846359574 scopus 로고    scopus 로고
    • Coassembling peptide-based biomaterials: effects of pairing equal and unequal chain length oligopeptides
    • Ramachandran S, Trewhella J, Tseng Y, Yu YB. Coassembling peptide-based biomaterials: effects of pairing equal and unequal chain length oligopeptides. Chem Mater 2006, 18:6157-6162.
    • (2006) Chem Mater , vol.18 , pp. 6157-6162
    • Ramachandran, S.1    Trewhella, J.2    Tseng, Y.3    Yu, Y.B.4
  • 156
    • 84877771266 scopus 로고    scopus 로고
    • Effect of enzyme concentration of the morphology and properties of enzymatically triggered peptide hydrogels
    • Guilbaud JB, Rochas C, Miller AF, Saiani A. Effect of enzyme concentration of the morphology and properties of enzymatically triggered peptide hydrogels. Biomacromolecules 2013, 14:1403-1411.
    • (2013) Biomacromolecules , vol.14 , pp. 1403-1411
    • Guilbaud, J.B.1    Rochas, C.2    Miller, A.F.3    Saiani, A.4
  • 157
    • 84876207293 scopus 로고    scopus 로고
    • Mussel inspired dynamic cross-linking of self-healing peptide nanofiber network
    • Ceylan H, Urel M, Erkal TS, Tekinay AB, Dana A, Guler MO. Mussel inspired dynamic cross-linking of self-healing peptide nanofiber network. Adv Funct Mater 2013, 23:2081-2090.
    • (2013) Adv Funct Mater , vol.23 , pp. 2081-2090
    • Ceylan, H.1    Urel, M.2    Erkal, T.S.3    Tekinay, A.B.4    Dana, A.5    Guler, M.O.6
  • 159
    • 0034837622 scopus 로고    scopus 로고
    • Hybrid hydrogels cross-linked by genetically engineered coiled-coil block proteins
    • Wang C, Kopecek J, Stewart RJ. Hybrid hydrogels cross-linked by genetically engineered coiled-coil block proteins. Biomacromolecules 2001, 2:912-920.
    • (2001) Biomacromolecules , vol.2 , pp. 912-920
    • Wang, C.1    Kopecek, J.2    Stewart, R.J.3
  • 160
    • 0033521939 scopus 로고    scopus 로고
    • Hybrid hydrogels assembled from synthetic polymers and coiled-coil protein domains
    • Wang C, Stewart RJ, Kopecek J. Hybrid hydrogels assembled from synthetic polymers and coiled-coil protein domains. Nature 1999, 397:417-420.
    • (1999) Nature , vol.397 , pp. 417-420
    • Wang, C.1    Stewart, R.J.2    Kopecek, J.3
  • 161
    • 40549145915 scopus 로고    scopus 로고
    • Genetically engineered block copolymers: influence of the length and structure of the coiled-coil blocks on hydrogel self-assembly
    • Xu C, Kopecek J. Genetically engineered block copolymers: influence of the length and structure of the coiled-coil blocks on hydrogel self-assembly. Pharm Res 2008, 25:674-682.
    • (2008) Pharm Res , vol.25 , pp. 674-682
    • Xu, C.1    Kopecek, J.2
  • 162
    • 55349084421 scopus 로고    scopus 로고
    • Novel synthesis of HPMA copolymers containing peptide grafts and their self-assembly into hybrid hydrogels
    • Wu K, Yang J, Konak C, Kopeckova P, Kopecek J. Novel synthesis of HPMA copolymers containing peptide grafts and their self-assembly into hybrid hydrogels. Macromol Chem Phys 2008, 209:467-475.
    • (2008) Macromol Chem Phys , vol.209 , pp. 467-475
    • Wu, K.1    Yang, J.2    Konak, C.3    Kopeckova, P.4    Kopecek, J.5
  • 163
    • 70449397517 scopus 로고    scopus 로고
    • Peptide/protein-synthetic polymer conjugates: Quo Vadis
    • Klok H-A. Peptide/protein-synthetic polymer conjugates: Quo Vadis. Macromolecules 2009, 42:7990-8000.
    • (2009) Macromolecules , vol.42 , pp. 7990-8000
    • Klok, H.-A.1
  • 164
    • 31744435118 scopus 로고    scopus 로고
    • Tuning the erosion rate of artificial protein hydrogels through control of network topology
    • Shen W, Zhang KC, Kornfield JA, Tirrell DA. Tuning the erosion rate of artificial protein hydrogels through control of network topology. Nat Mater 2006, 5:153-158.
    • (2006) Nat Mater , vol.5 , pp. 153-158
    • Shen, W.1    Zhang, K.C.2    Kornfield, J.A.3    Tirrell, D.A.4
  • 165
    • 33847026404 scopus 로고    scopus 로고
    • Dynamic properties of artificial protein hydrogels assembled through aggregation of leucine zipper peptide domains
    • Shen W, Kornfield JA, Tirrell DA. Dynamic properties of artificial protein hydrogels assembled through aggregation of leucine zipper peptide domains. Macromolecules 2007, 40:689-692.
    • (2007) Macromolecules , vol.40 , pp. 689-692
    • Shen, W.1    Kornfield, J.A.2    Tirrell, D.A.3
  • 166
    • 18744373049 scopus 로고    scopus 로고
    • Assembly of an artificial protein hydrogel through leucine zipper aggregation and disulfide bond formation
    • Shen W, Lammertink RGH, Sakata JK, Kornfield JA, Tirrell DA. Assembly of an artificial protein hydrogel through leucine zipper aggregation and disulfide bond formation. Macromolecules 2005, 38:3909-3916.
    • (2005) Macromolecules , vol.38 , pp. 3909-3916
    • Shen, W.1    Lammertink, R.G.H.2    Sakata, J.K.3    Kornfield, J.A.4    Tirrell, D.A.5
  • 167
    • 33845518485 scopus 로고    scopus 로고
    • Structure and mechanical properties of artificial protein hydrogels assembled through aggregation of leucine zipper peptide domains
    • Shen W, Kornfield JA, Tirrell DA. Structure and mechanical properties of artificial protein hydrogels assembled through aggregation of leucine zipper peptide domains. Soft Matter 2007, 3:99-107.
    • (2007) Soft Matter , vol.3 , pp. 99-107
    • Shen, W.1    Kornfield, J.A.2    Tirrell, D.A.3
  • 168
    • 79956315890 scopus 로고    scopus 로고
    • Hybrid hydrogels self-assembled from graft copolymers containing complementary β-sheets as hydroxyapatite nucleation scaffolds
    • Wu LC, Yang JY, Kopecek J. Hybrid hydrogels self-assembled from graft copolymers containing complementary β-sheets as hydroxyapatite nucleation scaffolds. Biomaterials 2011, 32:5341-5353.
    • (2011) Biomaterials , vol.32 , pp. 5341-5353
    • Wu, L.C.1    Yang, J.Y.2    Kopecek, J.3
  • 169
    • 0037155826 scopus 로고    scopus 로고
    • A designed system for assessing how sequence affects α to β conformational transitions in proteins
    • Ciani B, Hutchinson EG, Sessions RB, Woolfson DN. A designed system for assessing how sequence affects α to β conformational transitions in proteins. J Biol Chem 2002, 277:10150-10155.
    • (2002) J Biol Chem , vol.277 , pp. 10150-10155
    • Ciani, B.1    Hutchinson, E.G.2    Sessions, R.B.3    Woolfson, D.N.4
  • 170
    • 0034254720 scopus 로고    scopus 로고
    • Sticky-end assembly of a designed peptide fiber provides insight into protein fibrillogenesis
    • Pandya MJ, Spooner GM, Sunde M, Thorpe JR, Rodger A, Woolfson DN. Sticky-end assembly of a designed peptide fiber provides insight into protein fibrillogenesis. Biochemistry 2000, 39:8728-8734.
    • (2000) Biochemistry , vol.39 , pp. 8728-8734
    • Pandya, M.J.1    Spooner, G.M.2    Sunde, M.3    Thorpe, J.R.4    Rodger, A.5    Woolfson, D.N.6
  • 172
    • 0037161668 scopus 로고    scopus 로고
    • Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles
    • Nowak AP, Breedveld V, Pakstis L, Ozbas B, Pine DJ, Pochan D, Deming TJ. Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles. Nature 2002, 417:424-428.
    • (2002) Nature , vol.417 , pp. 424-428
    • Nowak, A.P.1    Breedveld, V.2    Pakstis, L.3    Ozbas, B.4    Pine, D.J.5    Pochan, D.6    Deming, T.J.7
  • 173
    • 0037008098 scopus 로고    scopus 로고
    • SANS and cryo-TEM study of self-assembled diblock copolypeptide hydrogels with rich nano- through microscale morphology
    • Pochan DJ, Pakstis L, Ozbas B, Nowak AP, Deming TJ. SANS and cryo-TEM study of self-assembled diblock copolypeptide hydrogels with rich nano- through microscale morphology. Macromolecules 2002, 35:5358-5360.
    • (2002) Macromolecules , vol.35 , pp. 5358-5360
    • Pochan, D.J.1    Pakstis, L.2    Ozbas, B.3    Nowak, A.P.4    Deming, T.J.5
  • 174
    • 2542613793 scopus 로고    scopus 로고
    • Rheology of block copolypeptide solutions: hydrogels with tunable properties
    • Breedveld V, Nowak AP, Sato J, Deming TJ, Pine DJ. Rheology of block copolypeptide solutions: hydrogels with tunable properties. Macromolecules 2004, 37:3943-3953.
    • (2004) Macromolecules , vol.37 , pp. 3943-3953
    • Breedveld, V.1    Nowak, A.P.2    Sato, J.3    Deming, T.J.4    Pine, D.J.5
  • 175
    • 80053908372 scopus 로고    scopus 로고
    • In situ forming physical hydrogels for three-dimensional tissue morphogenesis
    • Liu Y, Liu B, Riesberg JJ, Shen W. In situ forming physical hydrogels for three-dimensional tissue morphogenesis. Macromol Biosci 2011, 11:1325-1330.
    • (2011) Macromol Biosci , vol.11 , pp. 1325-1330
    • Liu, Y.1    Liu, B.2    Riesberg, J.J.3    Shen, W.4
  • 176
    • 66149113351 scopus 로고    scopus 로고
    • Hybrid multicomponent hydrogels for tissue engineering
    • Jia X, Kiick KL. Hybrid multicomponent hydrogels for tissue engineering. Macromol Biosci 2009, 9:140-156.
    • (2009) Macromol Biosci , vol.9 , pp. 140-156
    • Jia, X.1    Kiick, K.L.2
  • 177
    • 0038388786 scopus 로고    scopus 로고
    • Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers
    • Urry DW. Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers. J Phys Chem B 1997, 101:11007-11028.
    • (1997) J Phys Chem B , vol.101 , pp. 11007-11028
    • Urry, D.W.1
  • 178
    • 2542628131 scopus 로고    scopus 로고
    • Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides
    • Meyer DE, Chilkoti A. Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides. Biomacromolecules 2004, 5:846-851.
    • (2004) Biomacromolecules , vol.5 , pp. 846-851
    • Meyer, D.E.1    Chilkoti, A.2
  • 179
    • 0036739152 scopus 로고    scopus 로고
    • Characterization of a genetically engineered elastin-like polypeptide for cartilaginous tissue repair
    • Betre H, Setton LA, Meyer DE, Chilkoti A. Characterization of a genetically engineered elastin-like polypeptide for cartilaginous tissue repair. Biomacromolecules 2002, 3:910-916.
    • (2002) Biomacromolecules , vol.3 , pp. 910-916
    • Betre, H.1    Setton, L.A.2    Meyer, D.E.3    Chilkoti, A.4
  • 180
    • 24044513316 scopus 로고    scopus 로고
    • Chondrocytic differentiation of human adipose-derived adult stem cells in elastin-like polypeptide
    • Betre H, Ong SR, Guilak F, Chilkoti A, Fermor B, Setton LA. Chondrocytic differentiation of human adipose-derived adult stem cells in elastin-like polypeptide. Biomaterials 2006, 27:91-99.
    • (2006) Biomaterials , vol.27 , pp. 91-99
    • Betre, H.1    Ong, S.R.2    Guilak, F.3    Chilkoti, A.4    Fermor, B.5    Setton, L.A.6
  • 181
    • 0029098921 scopus 로고
    • Mechanical-behavior of articular-cartilage in shear is altered by transection of the anterior cruciate ligament
    • Setton LA, Mow VC, Howell DS. Mechanical-behavior of articular-cartilage in shear is altered by transection of the anterior cruciate ligament. J Orthop Res 1995, 13:473-482.
    • (1995) J Orthop Res , vol.13 , pp. 473-482
    • Setton, L.A.1    Mow, V.C.2    Howell, D.S.3
  • 182
    • 31044449508 scopus 로고    scopus 로고
    • Synthesis and in vitro evaluation of enzymatically cross-linked elastin-like polypeptide gels for cartilaginous tissue repair
    • McHale MK, Setton LA, Chilkoti A. Synthesis and in vitro evaluation of enzymatically cross-linked elastin-like polypeptide gels for cartilaginous tissue repair. Tissue Eng 2005, 11:1768-1779.
    • (2005) Tissue Eng , vol.11 , pp. 1768-1779
    • McHale, M.K.1    Setton, L.A.2    Chilkoti, A.3
  • 183
    • 0035860017 scopus 로고    scopus 로고
    • Mechanical properties of cross-linked synthetic elastomeric polypentapeptides
    • Lee J, Macosko CW, Urry DW. Mechanical properties of cross-linked synthetic elastomeric polypentapeptides. Macromolecules 2001, 34:5968-5974.
    • (2001) Macromolecules , vol.34 , pp. 5968-5974
    • Lee, J.1    Macosko, C.W.2    Urry, D.W.3
  • 184
    • 34249867928 scopus 로고    scopus 로고
    • Rapid cross-linking of elastin-like polypeptides with (hydroxymethyl)phosphines in aqueous solution
    • Lim DW, Nettles DL, Setton LA, Chilkoti A. Rapid cross-linking of elastin-like polypeptides with (hydroxymethyl)phosphines in aqueous solution. Biomacromolecules 2007, 8:1463-1470.
    • (2007) Biomacromolecules , vol.8 , pp. 1463-1470
    • Lim, D.W.1    Nettles, D.L.2    Setton, L.A.3    Chilkoti, A.4
  • 185
    • 67651177418 scopus 로고    scopus 로고
    • Synthesis of highly porous crosslinked elastin hydrogels and their interaction with fibroblasts in vitro
    • Annabi N, Mithieux SM, Boughton EA, Ruys AJ, Weiss AS, Dehghani F. Synthesis of highly porous crosslinked elastin hydrogels and their interaction with fibroblasts in vitro. Biomaterials 2009, 30:4550-4557.
    • (2009) Biomaterials , vol.30 , pp. 4550-4557
    • Annabi, N.1    Mithieux, S.M.2    Boughton, E.A.3    Ruys, A.J.4    Weiss, A.S.5    Dehghani, F.6
  • 186
    • 0038517754 scopus 로고    scopus 로고
    • Swelling and mechanical behaviors of chemically cross-linked hydrogels of elastin-like polypeptides
    • Trabbic-Carlson K, Setton LA, Chilkoti A. Swelling and mechanical behaviors of chemically cross-linked hydrogels of elastin-like polypeptides. Biomacromolecules 2003, 4:572-580.
    • (2003) Biomacromolecules , vol.4 , pp. 572-580
    • Trabbic-Carlson, K.1    Setton, L.A.2    Chilkoti, A.3
  • 187
    • 0036469685 scopus 로고    scopus 로고
    • Thermoplastic elastomer hydrogels via self-assembly of an elastin-mimetic triblock polypeptide
    • Wright ER, McMillan RA, Cooper A, Apkarian RP, Conticello VP. Thermoplastic elastomer hydrogels via self-assembly of an elastin-mimetic triblock polypeptide. Adv Funct Mater 2002, 12:149-154.
    • (2002) Adv Funct Mater , vol.12 , pp. 149-154
    • Wright, E.R.1    McMillan, R.A.2    Cooper, A.3    Apkarian, R.P.4    Conticello, V.P.5
  • 190
    • 0037151322 scopus 로고    scopus 로고
    • Solute diffusion in genetically engineered silk-elastinlike protein polymer hydrogels
    • Dinerman AA, Cappello J, Ghandehari H, Hoag SW. Solute diffusion in genetically engineered silk-elastinlike protein polymer hydrogels. J Control Release 2002, 82:277-287.
    • (2002) J Control Release , vol.82 , pp. 277-287
    • Dinerman, A.A.1    Cappello, J.2    Ghandehari, H.3    Hoag, S.W.4
  • 191
    • 1642441833 scopus 로고    scopus 로고
    • In vitro and in vivo evaluation of recombinant silk-elastinlike hydrogels for cancer gene therapy
    • Megeed Z, Haider M, Li DQ, O'Malley BW, Cappello J, Ghandehari H. In vitro and in vivo evaluation of recombinant silk-elastinlike hydrogels for cancer gene therapy. J Control Release 2004, 94:433-445.
    • (2004) J Control Release , vol.94 , pp. 433-445
    • Megeed, Z.1    Haider, M.2    Li, D.Q.3    O'Malley, B.W.4    Cappello, J.5    Ghandehari, H.6
  • 192
    • 0035997328 scopus 로고    scopus 로고
    • Controlled release of plasmid DNA from a genetically engineered silk-elastinlike hydrogel
    • Megeed Z, Cappello J, Ghandehari H. Controlled release of plasmid DNA from a genetically engineered silk-elastinlike hydrogel. Pharm Res 2002, 19:954-959.
    • (2002) Pharm Res , vol.19 , pp. 954-959
    • Megeed, Z.1    Cappello, J.2    Ghandehari, H.3
  • 193
    • 33947143774 scopus 로고    scopus 로고
    • Adenoviral gene delivery to solid tumors by recombinant silk-elastinlike protein polymers
    • Hatefi A, Cappello J, Ghandehari H. Adenoviral gene delivery to solid tumors by recombinant silk-elastinlike protein polymers. Pharm Res 2007, 24:773-779.
    • (2007) Pharm Res , vol.24 , pp. 773-779
    • Hatefi, A.1    Cappello, J.2    Ghandehari, H.3
  • 195
    • 84864994876 scopus 로고    scopus 로고
    • Rheological properties of cysteine-containing elastin-like polypeptide solutions and hydrogels
    • Xu DH, Asai D, Chilkoti A, Craig SL. Rheological properties of cysteine-containing elastin-like polypeptide solutions and hydrogels. Biomacromolecules 2012, 13:2315-2321.
    • (2012) Biomacromolecules , vol.13 , pp. 2315-2321
    • Xu, D.H.1    Asai, D.2    Chilkoti, A.3    Craig, S.L.4
  • 196
    • 28444469746 scopus 로고    scopus 로고
    • Gelatin as a delivery vehicle for the controlled release of bioactive molecules
    • Young S, Wong M, Tabata Y, Mikos AG. Gelatin as a delivery vehicle for the controlled release of bioactive molecules. J Control Release 2005, 109:256-274.
    • (2005) J Control Release , vol.109 , pp. 256-274
    • Young, S.1    Wong, M.2    Tabata, Y.3    Mikos, A.G.4
  • 197
    • 0032749668 scopus 로고    scopus 로고
    • Growth factor release from gelatin hydrogel for tissue engineering
    • Yamamoto M, Tabata Y, Ikada Y. Growth factor release from gelatin hydrogel for tissue engineering. J Bioact Compat Polym 1999, 14:474-489.
    • (1999) J Bioact Compat Polym , vol.14 , pp. 474-489
    • Yamamoto, M.1    Tabata, Y.2    Ikada, Y.3
  • 198
    • 44049122788 scopus 로고
    • Structure and rheology of gelatin gels - recent progress
    • Rossmurphy SB. Structure and rheology of gelatin gels - recent progress. Polymer 1992, 33:2622-2627.
    • (1992) Polymer , vol.33 , pp. 2622-2627
    • Rossmurphy, S.B.1
  • 199
    • 33845722198 scopus 로고    scopus 로고
    • On the nature of crosslinks in thermoreversible gels
    • Kt N. On the nature of crosslinks in thermoreversible gels. Polym Bull 2007, 58:27-42.
    • (2007) Polym Bull , vol.58 , pp. 27-42
    • Kt, N.1
  • 200
    • 84963158346 scopus 로고
    • Structural and mechanical-properties of bio-polymer gels
    • Clark AH, Rossmurphy SB. Structural and mechanical-properties of bio-polymer gels. Adv Polym Sci 1987, 83:57-192.
    • (1987) Adv Polym Sci , vol.83 , pp. 57-192
    • Clark, A.H.1    Rossmurphy, S.B.2
  • 201
    • 0033797890 scopus 로고    scopus 로고
    • Rheological characterisation of gelatins from mammalian and marine sources
    • Gilsenan PM, Ross-Murphy SB. Rheological characterisation of gelatins from mammalian and marine sources. Food Hydrocolloids 2000, 14:191-195.
    • (2000) Food Hydrocolloids , vol.14 , pp. 191-195
    • Gilsenan, P.M.1    Ross-Murphy, S.B.2
  • 202
    • 0034215958 scopus 로고    scopus 로고
    • Viscoelasticity of thermoreversible gelatin gels from mammalian and piscine collagens
    • Gilsenan PM, Ross-Murphy SB. Viscoelasticity of thermoreversible gelatin gels from mammalian and piscine collagens. J Rheol 2000, 44:871-883.
    • (2000) J Rheol , vol.44 , pp. 871-883
    • Gilsenan, P.M.1    Ross-Murphy, S.B.2
  • 203
    • 0035913424 scopus 로고    scopus 로고
    • Shear creep of gelatin gels from mammalian and piscine collagens
    • Gilsenan PM, Ross-Murphy SB. Shear creep of gelatin gels from mammalian and piscine collagens. Int J Biol Macromol 2001, 29:53-61.
    • (2001) Int J Biol Macromol , vol.29 , pp. 53-61
    • Gilsenan, P.M.1    Ross-Murphy, S.B.2
  • 205
    • 43949086047 scopus 로고    scopus 로고
    • Thermoreversible lysozyme hydrogels: properties and an insight into the gelation pathway
    • Yan H, Frielinghaus H, Nykanen A, Ruokolainen J, Saiani A, Miller AF. Thermoreversible lysozyme hydrogels: properties and an insight into the gelation pathway. Soft Matter 2008, 4:1313-1325.
    • (2008) Soft Matter , vol.4 , pp. 1313-1325
    • Yan, H.1    Frielinghaus, H.2    Nykanen, A.3    Ruokolainen, J.4    Saiani, A.5    Miller, A.F.6
  • 206
    • 33746073762 scopus 로고    scopus 로고
    • Food biophysics of protein gels: a challenge of nano and macroscopic proportions
    • Foegeding EA. Food biophysics of protein gels: a challenge of nano and macroscopic proportions. Food Biophys 2006, 1:41-50.
    • (2006) Food Biophys , vol.1 , pp. 41-50
    • Foegeding, E.A.1
  • 207
    • 0036468090 scopus 로고    scopus 로고
    • Aggregation, gelation and phase separation of heat denatured globular proteins
    • Durand D, Gimel JC, Nicolai T. Aggregation, gelation and phase separation of heat denatured globular proteins. Physica A 2002, 304:253-265.
    • (2002) Physica A , vol.304 , pp. 253-265
    • Durand, D.1    Gimel, J.C.2    Nicolai, T.3
  • 210
    • 0037126101 scopus 로고    scopus 로고
    • Novel amyloid fibrillar networks derived from a globular protein: β-lactoglobulin
    • Gosal WS, Clark AH, Pudney PDA, Ross-Murphy SB. Novel amyloid fibrillar networks derived from a globular protein: β-lactoglobulin. Langmuir 2002, 18:7174-7181.
    • (2002) Langmuir , vol.18 , pp. 7174-7181
    • Gosal, W.S.1    Clark, A.H.2    Pudney, P.D.A.3    Ross-Murphy, S.B.4
  • 211
    • 9744282630 scopus 로고    scopus 로고
    • Fibrillar β-lactoglobulin gels: Part 2. Dynamic mechanical characterization of heat-set systems
    • Gosal WS, Clark AH, Ross-Murphy SB. Fibrillar β-lactoglobulin gels: Part 2. Dynamic mechanical characterization of heat-set systems. Biomacromolecules 2004, 5:2420-2429.
    • (2004) Biomacromolecules , vol.5 , pp. 2420-2429
    • Gosal, W.S.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 212
    • 9744255442 scopus 로고    scopus 로고
    • Fibrillar β-lactoglobulin gels: Part 3. Dynamic mechanical of solvent-induced systems
    • Gosal WS, Clark AH, Ross-Murphy SB. Fibrillar β-lactoglobulin gels: Part 3. Dynamic mechanical of solvent-induced systems. Biomacromolecules 2004, 5:2430-2438.
    • (2004) Biomacromolecules , vol.5 , pp. 2430-2438
    • Gosal, W.S.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 213
    • 0034318911 scopus 로고    scopus 로고
    • Heat-induced gelation of globular proteins: 4. Gelation kinetics of low pH β-lactoglobulin gels
    • Kavanagh GM, Clark AH, Ross-Murphy SB. Heat-induced gelation of globular proteins: 4. Gelation kinetics of low pH β-lactoglobulin gels. Langmuir 2000, 16:9584-9594.
    • (2000) Langmuir , vol.16 , pp. 9584-9594
    • Kavanagh, G.M.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 214
    • 0031208028 scopus 로고    scopus 로고
    • Heat-induced gelation of globular proteins. 2. Effect of environmental factors on single-component and mixed-protein gels
    • Tobitani A, RossMurphy SB. Heat-induced gelation of globular proteins. 2. Effect of environmental factors on single-component and mixed-protein gels. Macromolecules 1997, 30:4855-4862.
    • (1997) Macromolecules , vol.30 , pp. 4855-4862
    • Tobitani, A.1    RossMurphy, S.B.2
  • 215
    • 1242310516 scopus 로고    scopus 로고
    • Mesoscopic properties of semiflexible amyloid fibrils
    • Sagis LMC, Veerman C, van der Linden E. Mesoscopic properties of semiflexible amyloid fibrils. Langmuir 2004, 20:924-927.
    • (2004) Langmuir , vol.20 , pp. 924-927
    • Sagis, L.M.C.1    Veerman, C.2    van der Linden, E.3
  • 216
    • 0036054901 scopus 로고    scopus 로고
    • Effect of electrostatic interactions on the percolation concentration of fibrillar β-lactoglobulin gels
    • Veerman C, Ruis H, Sagis LMC, van der Linden E. Effect of electrostatic interactions on the percolation concentration of fibrillar β-lactoglobulin gels. Biomacromolecules 2002, 3:869-873.
    • (2002) Biomacromolecules , vol.3 , pp. 869-873
    • Veerman, C.1    Ruis, H.2    Sagis, L.M.C.3    van der Linden, E.4
  • 217
    • 0242352388 scopus 로고    scopus 로고
    • Irreversible self-assembly of ovalbumin into fibrils and the resulting network rheology
    • Veerman C, de Schiffart G, Sagis LMC, van der Linden E. Irreversible self-assembly of ovalbumin into fibrils and the resulting network rheology. Int J Biol Macromol 2003, 33:121-127.
    • (2003) Int J Biol Macromol , vol.33 , pp. 121-127
    • Veerman, C.1    de Schiffart, G.2    Sagis, L.M.C.3    van der Linden, E.4
  • 219
    • 6444224496 scopus 로고    scopus 로고
    • Dynamic mechanical characterization of the heat-induced formation of fractal globular protein gels
    • Pouzot M, Benyahia L, Nicolai T. Dynamic mechanical characterization of the heat-induced formation of fractal globular protein gels. J Rheol 2004, 48:1123-1134.
    • (2004) J Rheol , vol.48 , pp. 1123-1134
    • Pouzot, M.1    Benyahia, L.2    Nicolai, T.3
  • 220
    • 9744278424 scopus 로고    scopus 로고
    • Influence of the ionic strength on the structure of heat-set globular protein gels at pH 7. β-Lactoglobulin
    • Pouzot M, Durand D, Nicolai T. Influence of the ionic strength on the structure of heat-set globular protein gels at pH 7. β-Lactoglobulin. Macromolecules 2004, 37:8703-8708.
    • (2004) Macromolecules , vol.37 , pp. 8703-8708
    • Pouzot, M.1    Durand, D.2    Nicolai, T.3
  • 221
    • 0442326631 scopus 로고    scopus 로고
    • Structure factor and elasticity of a heat-set globular protein gel
    • Pouzot M, Nicolai T, Durand D, Benyahia L. Structure factor and elasticity of a heat-set globular protein gel. Macromolecules 2004, 37:614-620.
    • (2004) Macromolecules , vol.37 , pp. 614-620
    • Pouzot, M.1    Nicolai, T.2    Durand, D.3    Benyahia, L.4
  • 222
    • 48949098052 scopus 로고    scopus 로고
    • Light scattering study of heat-denatured globular protein aggregates
    • Mehalebi S, Nicolai T, Durand D. Light scattering study of heat-denatured globular protein aggregates. Int J Biol Macromol 2008, 43:129-135.
    • (2008) Int J Biol Macromol , vol.43 , pp. 129-135
    • Mehalebi, S.1    Nicolai, T.2    Durand, D.3
  • 223
    • 41149173263 scopus 로고    scopus 로고
    • The influence of electrostatic interaction on the structure and the shear modulus of heat-set globular protein gels
    • Mehalebi S, Nicolai T, Durand D. The influence of electrostatic interaction on the structure and the shear modulus of heat-set globular protein gels. Soft Matter 2008, 4:893-900.
    • (2008) Soft Matter , vol.4 , pp. 893-900
    • Mehalebi, S.1    Nicolai, T.2    Durand, D.3
  • 225
    • 3142651429 scopus 로고    scopus 로고
    • Polymerization and gelation of whey protein isolates at Low pH using transglutaminase enzyme
    • Eissa AS, Bisram S, Khan SA. Polymerization and gelation of whey protein isolates at Low pH using transglutaminase enzyme. J Agric Food Chem 2004, 52:4456-4464.
    • (2004) J Agric Food Chem , vol.52 , pp. 4456-4464
    • Eissa, A.S.1    Bisram, S.2    Khan, S.A.3
  • 226
    • 21644432768 scopus 로고    scopus 로고
    • Acid-induced gelation of enzymatically modified, preheated whey proteins
    • Eissa AS, Khan SA. Acid-induced gelation of enzymatically modified, preheated whey proteins. J Agric Food Chem 2005, 53:5010-5017.
    • (2005) J Agric Food Chem , vol.53 , pp. 5010-5017
    • Eissa, A.S.1    Khan, S.A.2
  • 227
    • 77956110154 scopus 로고    scopus 로고
    • Formation of elastic whey protein gels at low pH by acid equilibration
    • Vardhanabhuti B, Khayankan W, Foegeding EA. Formation of elastic whey protein gels at low pH by acid equilibration. J Food Sci 2010, 75:E305-E313.
    • (2010) J Food Sci , vol.75 , pp. E305-E313
    • Vardhanabhuti, B.1    Khayankan, W.2    Foegeding, E.A.3
  • 228
    • 0030875449 scopus 로고    scopus 로고
    • Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties
    • Pins GD, Christiansen DL, Patel R, Silver FH. Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties. Biophys J 1997, 73:2164-2172.
    • (1997) Biophys J , vol.73 , pp. 2164-2172
    • Pins, G.D.1    Christiansen, D.L.2    Patel, R.3    Silver, F.H.4
  • 230
    • 9644257302 scopus 로고    scopus 로고
    • De novo engineering of reticular connective tissue in vivo by silk fibroin nonwoven materials
    • Dal Pra I, Freddi G, Minic J, Chiarini A, Armato U. De novo engineering of reticular connective tissue in vivo by silk fibroin nonwoven materials. Biomaterials 2005, 26:1987-1999.
    • (2005) Biomaterials , vol.26 , pp. 1987-1999
    • Dal Pra, I.1    Freddi, G.2    Minic, J.3    Chiarini, A.4    Armato, U.5
  • 232
    • 0942279251 scopus 로고    scopus 로고
    • Biodegradation of Bombyx mori silk fibroin fibers and films
    • Arai T, Freddi G, Innocenti R, Tsukada M. Biodegradation of Bombyx mori silk fibroin fibers and films. J Appl Polym Sci 2004, 91:2383-2390.
    • (2004) J Appl Polym Sci , vol.91 , pp. 2383-2390
    • Arai, T.1    Freddi, G.2    Innocenti, R.3    Tsukada, M.4
  • 235
    • 4043074966 scopus 로고    scopus 로고
    • Fibroin hydrogels for biomedical applications: preparation, characterization and in vitro cell culture studies
    • Motta A, Migliaresi C, Faccioni F, Torricelli P, Fini M, Giardino R. Fibroin hydrogels for biomedical applications: preparation, characterization and in vitro cell culture studies. J Biomater Sci Polym Ed 2004, 15:851-864.
    • (2004) J Biomater Sci Polym Ed , vol.15 , pp. 851-864
    • Motta, A.1    Migliaresi, C.2    Faccioni, F.3    Torricelli, P.4    Fini, M.5    Giardino, R.6
  • 236
    • 28844454988 scopus 로고    scopus 로고
    • Swelling behavior and morphological evolution of mixed gelatin/silk fibroin hydrogels
    • Gil ES, Frankowski DJ, Spontak RJ, Hudson SM. Swelling behavior and morphological evolution of mixed gelatin/silk fibroin hydrogels. Biomacromolecules 2005, 6:3079-3087.
    • (2005) Biomacromolecules , vol.6 , pp. 3079-3087
    • Gil, E.S.1    Frankowski, D.J.2    Spontak, R.J.3    Hudson, S.M.4
  • 237
    • 24144473879 scopus 로고    scopus 로고
    • Effect of β-sheet crystals on the thermal and rheological behavior of protein-based hydrogels derived from gelatin and silk fibroin
    • Gil ES, Spontak RJ, Hudson SM. Effect of β-sheet crystals on the thermal and rheological behavior of protein-based hydrogels derived from gelatin and silk fibroin. Macromol Biosci 2005, 5:702-709.
    • (2005) Macromol Biosci , vol.5 , pp. 702-709
    • Gil, E.S.1    Spontak, R.J.2    Hudson, S.M.3
  • 238
    • 0034704173 scopus 로고    scopus 로고
    • Silk fibroin of Bombyx mori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6 : 6 : 1 molar ratio
    • Inoue S, Tanaka K, Arisaka F, Kimura S, Ohtomo K, Mizuno S. Silk fibroin of Bombyx mori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6 : 6 : 1 molar ratio. J Biol Chem 2000, 275:40517-40528.
    • (2000) J Biol Chem , vol.275 , pp. 40517-40528
    • Inoue, S.1    Tanaka, K.2    Arisaka, F.3    Kimura, S.4    Ohtomo, K.5    Mizuno, S.6
  • 242
    • 10044274310 scopus 로고    scopus 로고
    • Three-dimensional aqueous-derived biomaterial scaffolds from silk fibroin
    • Kim UJ, Park J, Kim HJ, Wada M, Kaplan DL. Three-dimensional aqueous-derived biomaterial scaffolds from silk fibroin. Biomaterials 2005, 26:2775-2785.
    • (2005) Biomaterials , vol.26 , pp. 2775-2785
    • Kim, U.J.1    Park, J.2    Kim, H.J.3    Wada, M.4    Kaplan, D.L.5
  • 243
    • 2542588554 scopus 로고    scopus 로고
    • Porous 3-D scaffolds from regenerated silk fibroin
    • Nazarov R, Jin HJ, Kaplan DL. Porous 3-D scaffolds from regenerated silk fibroin. Biomacromolecules 2004, 5:718-726.
    • (2004) Biomacromolecules , vol.5 , pp. 718-726
    • Nazarov, R.1    Jin, H.J.2    Kaplan, D.L.3
  • 244
    • 70350028288 scopus 로고    scopus 로고
    • Vortex-induced injectable silk fibroin hydrogels
    • Yucel T, Cebe P, Kaplan DL. Vortex-induced injectable silk fibroin hydrogels. Biophys J 2009, 97:2044-2050.
    • (2009) Biophys J , vol.97 , pp. 2044-2050
    • Yucel, T.1    Cebe, P.2    Kaplan, D.L.3
  • 245
    • 22044444149 scopus 로고    scopus 로고
    • A study on the flow stability of regenerated silk fibroin aqueous solution
    • Wang H, Zhang YP, Shao HL, Hu XC. A study on the flow stability of regenerated silk fibroin aqueous solution. Int J Biol Macromol 2005, 36:66-70.
    • (2005) Int J Biol Macromol , vol.36 , pp. 66-70
    • Wang, H.1    Zhang, Y.P.2    Shao, H.L.3    Hu, X.C.4
  • 246
    • 37349055201 scopus 로고    scopus 로고
    • Sonication-induced gelation of silk fibroin for cell encapsulation
    • Wang X, Kluge JA, Leisk GG, Kaplan DL. Sonication-induced gelation of silk fibroin for cell encapsulation. Biomaterials 2008, 29:1054-1064.
    • (2008) Biomaterials , vol.29 , pp. 1054-1064
    • Wang, X.1    Kluge, J.A.2    Leisk, G.G.3    Kaplan, D.L.4
  • 247
    • 0032492935 scopus 로고    scopus 로고
    • Silk production in a spider involves acid bath treatment
    • Vollrath F, Knight DP, Hu XW. Silk production in a spider involves acid bath treatment. Proc R Soc B Biol Sci 1998, 265:817-820.
    • (1998) Proc R Soc B Biol Sci , vol.265 , pp. 817-820
    • Vollrath, F.1    Knight, D.P.2    Hu, X.W.3
  • 249
    • 28544444167 scopus 로고    scopus 로고
    • Rheological characterization of hydrogels formed by recombinantly produced spider silk
    • Rammensee S, Huemmerich D, Hermanson KD, Scheibel T, Bausch AR. Rheological characterization of hydrogels formed by recombinantly produced spider silk. Appl Phys A 2006, 82:261-264.
    • (2006) Appl Phys A , vol.82 , pp. 261-264
    • Rammensee, S.1    Huemmerich, D.2    Hermanson, K.D.3    Scheibel, T.4    Bausch, A.R.5
  • 250
  • 251
    • 0242551681 scopus 로고    scopus 로고
    • Biopolymeric delivery matrices for angiogenic growth factors
    • Zisch AH, Lutolf MP, Hubbell JA. Biopolymeric delivery matrices for angiogenic growth factors. Cardiovasc Pathol 2003, 12:295-310.
    • (2003) Cardiovasc Pathol , vol.12 , pp. 295-310
    • Zisch, A.H.1    Lutolf, M.P.2    Hubbell, J.A.3
  • 252
    • 4544382421 scopus 로고    scopus 로고
    • Preparation of semi-interpenetrating polymer networks composed of silk fibroin and poloxamer macromer
    • Yoo MK, Kweon HY, Lee KG, Lee HC, Cho CS. Preparation of semi-interpenetrating polymer networks composed of silk fibroin and poloxamer macromer. Int J Biol Macromol 2004, 34:263-270.
    • (2004) Int J Biol Macromol , vol.34 , pp. 263-270
    • Yoo, M.K.1    Kweon, H.Y.2    Lee, K.G.3    Lee, H.C.4    Cho, C.S.5
  • 253
    • 0017157722 scopus 로고
    • Rheological measurements of fibrin gels during clotting
    • Fukada E, Kaibara M. Rheological measurements of fibrin gels during clotting. Thromb Res 1976, 8:49-58.
    • (1976) Thromb Res , vol.8 , pp. 49-58
    • Fukada, E.1    Kaibara, M.2
  • 254
    • 0017732351 scopus 로고
    • Fukada E. Effect of temperature on dynamic viscoelasticity during clotting reaction of fibrin
    • Kaibara M. Fukada E. Effect of temperature on dynamic viscoelasticity during clotting reaction of fibrin. Biochim Biophys Acta 1977, 499:352-361.
    • (1977) Biochim Biophys Acta , vol.499 , pp. 352-361
    • Kaibara, M.1
  • 255
    • 0019206665 scopus 로고
    • An analysis of the clotting curves of complex dynamic rigidity for fibrinogen-thrombin solutions
    • Kaibara M, Fukada E. An analysis of the clotting curves of complex dynamic rigidity for fibrinogen-thrombin solutions. Biorheology 1980, 17:255-259.
    • (1980) Biorheology , vol.17 , pp. 255-259
    • Kaibara, M.1    Fukada, E.2
  • 256
    • 0022259737 scopus 로고
    • A new rheological method to measure fluidity change of blood during coagulation - application to invitro evaluation of anticoagulability of artificial materials
    • Kaibara M, Date M. A new rheological method to measure fluidity change of blood during coagulation - application to invitro evaluation of anticoagulability of artificial materials. Biorheology 1985, 22:197-208.
    • (1985) Biorheology , vol.22 , pp. 197-208
    • Kaibara, M.1    Date, M.2
  • 258
    • 0032750788 scopus 로고    scopus 로고
    • Influence of a natural and a synthetic inhibitor of factor XIIIa on fibrin clot rheology
    • Ryan EA, Mockros LF, Stern AM, Lorand L. Influence of a natural and a synthetic inhibitor of factor XIIIa on fibrin clot rheology. Biophys J 1999, 77:2827-2836.
    • (1999) Biophys J , vol.77 , pp. 2827-2836
    • Ryan, E.A.1    Mockros, L.F.2    Stern, A.M.3    Lorand, L.4
  • 259
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • Hartgerink JD, Beniash E, Stupp SI. Self-assembly and mineralization of peptide-amphiphile nanofibers. Science 2001, 294:1684-1688.
    • (2001) Science , vol.294 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 262
    • 0038789021 scopus 로고    scopus 로고
    • Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction
    • Niece KL, Hartgerink JD, Donners J, Stupp SI. Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction. J Am Chem Soc 2003, 125:7146-7147.
    • (2003) J Am Chem Soc , vol.125 , pp. 7146-7147
    • Niece, K.L.1    Hartgerink, J.D.2    Donners, J.3    Stupp, S.I.4
  • 263
    • 13644268564 scopus 로고    scopus 로고
    • Coassembly of amphiphiles with opposite peptide polarities into nanofibers
    • Behanna HA, Donners J, Gordon AC, Stupp SI. Coassembly of amphiphiles with opposite peptide polarities into nanofibers. J Am Chem Soc 2005, 127:1193-1200.
    • (2005) J Am Chem Soc , vol.127 , pp. 1193-1200
    • Behanna, H.A.1    Donners, J.2    Gordon, A.C.3    Stupp, S.I.4
  • 265
    • 12844286898 scopus 로고    scopus 로고
    • Self-assembled peptide amphiphile nanofibers conjugated to MRI contrast agents
    • Bull SR, Guler MO, Bras RE, Meade TJ, Stupp SI. Self-assembled peptide amphiphile nanofibers conjugated to MRI contrast agents. Nano Lett 2005, 5:1-4.
    • (2005) Nano Lett , vol.5 , pp. 1-4
    • Bull, S.R.1    Guler, M.O.2    Bras, R.E.3    Meade, T.J.4    Stupp, S.I.5
  • 266
    • 44349108852 scopus 로고    scopus 로고
    • Peptide amphiphile nanostructure-heparin interactions and their relationship to bioactivity
    • Rajangam K, Arnold MS, Rocco MA, Stupp SI. Peptide amphiphile nanostructure-heparin interactions and their relationship to bioactivity. Biomaterials 2008, 29:3298-3305.
    • (2008) Biomaterials , vol.29 , pp. 3298-3305
    • Rajangam, K.1    Arnold, M.S.2    Rocco, M.A.3    Stupp, S.I.4
  • 269
    • 0037117498 scopus 로고    scopus 로고
    • Peptide-amphiphile nanofibers: a versatile scaffold for the preparation of self-assembling materials
    • Hartgerink JD, Beniash E, Stupp SI. Peptide-amphiphile nanofibers: a versatile scaffold for the preparation of self-assembling materials. Proc Natl Acad Sci U S A 2002, 99:5133-5138.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 5133-5138
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 270
    • 27744574720 scopus 로고    scopus 로고
    • Enzyme-mediated degradation of peptide-amphiphile nanofiber networks
    • Jun HW, Yuwono V, Paramonov SE, Hartgerink JD. Enzyme-mediated degradation of peptide-amphiphile nanofiber networks. Adv Mater 2005, 17:2612-2617.
    • (2005) Adv Mater , vol.17 , pp. 2612-2617
    • Jun, H.W.1    Yuwono, V.2    Paramonov, S.E.3    Hartgerink, J.D.4
  • 271
    • 77951682263 scopus 로고    scopus 로고
    • Tuning supramolecular rigidity of peptide fibers through molecular structure
    • Pashuck ET, Cui HG, Stupp SI. Tuning supramolecular rigidity of peptide fibers through molecular structure. J Am Chem Soc 2010, 132:6041-6046.
    • (2010) J Am Chem Soc , vol.132 , pp. 6041-6046
    • Pashuck, E.T.1    Cui, H.G.2    Stupp, S.I.3
  • 273
    • 79551681262 scopus 로고    scopus 로고
    • Electrostatic effects on nanofiber formation of self-assembling peptide amphiphiles
    • Toksoz S, Mammadov R, Tekinay AB, Guler MO. Electrostatic effects on nanofiber formation of self-assembling peptide amphiphiles. J Colloid Interface Sci 2011, 356:131-137.
    • (2011) J Colloid Interface Sci , vol.356 , pp. 131-137
    • Toksoz, S.1    Mammadov, R.2    Tekinay, A.B.3    Guler, M.O.4
  • 274
    • 33644913129 scopus 로고    scopus 로고
    • Nanostructured hydrogels for three-dimensional cell culture through self-assembly of fluorenylmethoxycarbonyl-dipeptides
    • Jayawarna V, Ali M, Jowitt TA, Miller AE, Saiani A, Gough JE, Ulijn RV. Nanostructured hydrogels for three-dimensional cell culture through self-assembly of fluorenylmethoxycarbonyl-dipeptides. Adv Mater 2006, 18:611-614.
    • (2006) Adv Mater , vol.18 , pp. 611-614
    • Jayawarna, V.1    Ali, M.2    Jowitt, T.A.3    Miller, A.E.4    Saiani, A.5    Gough, J.E.6    Ulijn, R.V.7
  • 277
    • 34247212835 scopus 로고    scopus 로고
    • In vitro and in vivo enzymatic formation of supramolecular hydrogels based on self-assembled nanofibers of a β-amino acid derivative
    • Yang Z, Liang G, Ma M, Gao Y, Xu B. In vitro and in vivo enzymatic formation of supramolecular hydrogels based on self-assembled nanofibers of a β-amino acid derivative. Small 2007, 3:558-562.
    • (2007) Small , vol.3 , pp. 558-562
    • Yang, Z.1    Liang, G.2    Ma, M.3    Gao, Y.4    Xu, B.5
  • 278
    • 25444531477 scopus 로고    scopus 로고
    • Self-assembly of small molecules affords multifunctional supramolecular hydrogels for topically treating simulated uranium wounds
    • Yang ZM, Xu KM, Wang L, Gu HW, Wei H, Zhang MJ, Xu B. Self-assembly of small molecules affords multifunctional supramolecular hydrogels for topically treating simulated uranium wounds. Chem Commun 2005, XX:4414-4416.
    • (2005) Chem Commun , vol.20 , pp. 4414-4416
    • Yang, Z.M.1    Xu, K.M.2    Wang, L.3    Gu, H.W.4    Wei, H.5    Zhang, M.J.6    Xu, B.7
  • 279
    • 69949150597 scopus 로고    scopus 로고
    • Controlled release from modified amino acid hydrogels governed by molecular size or network dynamics
    • Sutton S, Campbell NL, Cooper AI, Kirkland M, Frith WJ, Adams DJ. Controlled release from modified amino acid hydrogels governed by molecular size or network dynamics. Langmuir 2009, 25:10285-10291.
    • (2009) Langmuir , vol.25 , pp. 10285-10291
    • Sutton, S.1    Campbell, N.L.2    Cooper, A.I.3    Kirkland, M.4    Frith, W.J.5    Adams, D.J.6
  • 282
    • 33644944179 scopus 로고    scopus 로고
    • Using a kinase/phosphatase switch to regulate a supramolecular hydrogel and forming the supramoleclar hydrogel in vivo
    • Yang ZM, Liang GL, Wang L, Xu B. Using a kinase/phosphatase switch to regulate a supramolecular hydrogel and forming the supramoleclar hydrogel in vivo. J Am Chem Soc 2006, 128:3038-3043.
    • (2006) J Am Chem Soc , vol.128 , pp. 3038-3043
    • Yang, Z.M.1    Liang, G.L.2    Wang, L.3    Xu, B.4
  • 283
    • 65349180766 scopus 로고    scopus 로고
    • A new method for maintaining homogeneity during liquid-hydrogel transitions using low molecular weight hydrogelators
    • Adams DJ, Butler MF, Frith WJ, Kirkland M, Mullen L, Sanderson P. A new method for maintaining homogeneity during liquid-hydrogel transitions using low molecular weight hydrogelators. Soft Matter 2009, 5:1856-1862.
    • (2009) Soft Matter , vol.5 , pp. 1856-1862
    • Adams, D.J.1    Butler, M.F.2    Frith, W.J.3    Kirkland, M.4    Mullen, L.5    Sanderson, P.6
  • 284
    • 33745152345 scopus 로고    scopus 로고
    • Rigid, self-assembled hydrogel composed of a modified aromatic dipeptide
    • Mahler A, Reches M, Rechter M, Cohen S, Gazit E. Rigid, self-assembled hydrogel composed of a modified aromatic dipeptide. Adv Mater 2006, 18:1365-1370.
    • (2006) Adv Mater , vol.18 , pp. 1365-1370
    • Mahler, A.1    Reches, M.2    Rechter, M.3    Cohen, S.4    Gazit, E.5
  • 285
    • 70349333612 scopus 로고    scopus 로고
    • Controlling stiffness in nanostructured hydrogels produced by enzymatic dephosphorylation
    • Thornton K, Smith AM, Merry CLR, Ulijn RV. Controlling stiffness in nanostructured hydrogels produced by enzymatic dephosphorylation. Biochem Soc Trans 2009, 37:660-664.
    • (2009) Biochem Soc Trans , vol.37 , pp. 660-664
    • Thornton, K.1    Smith, A.M.2    Merry, C.L.R.3    Ulijn, R.V.4
  • 286
    • 0242490652 scopus 로고    scopus 로고
    • Supramolecular hydrogels respond to ligand-receptor interaction
    • Zhang Y, Gu HW, Yang ZM, Xu B. Supramolecular hydrogels respond to ligand-receptor interaction. J Am Chem Soc 2003, 125:13680-13681.
    • (2003) J Am Chem Soc , vol.125 , pp. 13680-13681
    • Zhang, Y.1    Gu, H.W.2    Yang, Z.M.3    Xu, B.4
  • 287
    • 9344260876 scopus 로고    scopus 로고
    • Molecular recognition remolds the self-assembly of hydrogelators and increases the elasticity of the hydrogel by 10(6)-fold
    • Zhang Y, Yang ZM, Yuan F, Gu HW, Gao P, Xu B. Molecular recognition remolds the self-assembly of hydrogelators and increases the elasticity of the hydrogel by 10(6)-fold. J Am Chem Soc 2004, 126:15028-15029.
    • (2004) J Am Chem Soc , vol.126 , pp. 15028-15029
    • Zhang, Y.1    Yang, Z.M.2    Yuan, F.3    Gu, H.W.4    Gao, P.5    Xu, B.6
  • 288
    • 77951557215 scopus 로고    scopus 로고
    • Relationship between molecular structure, gelation behaviour and gel properties of Fmoc-dipeptides
    • Adams DJ, Mullen LM, Berta M, Chen L, Frith WJ. Relationship between molecular structure, gelation behaviour and gel properties of Fmoc-dipeptides. Soft Matter 2010, 6:1971-1980.
    • (2010) Soft Matter , vol.6 , pp. 1971-1980
    • Adams, D.J.1    Mullen, L.M.2    Berta, M.3    Chen, L.4    Frith, W.J.5
  • 290
    • 70349301456 scopus 로고    scopus 로고
    • Using matrix metalloprotease-9 (MMP-9) to trigger supramolecular hydrogelation
    • Yang Z, Ma M, Xu B. Using matrix metalloprotease-9 (MMP-9) to trigger supramolecular hydrogelation. Soft Matter 2009, 5:2546-2548.
    • (2009) Soft Matter , vol.5 , pp. 2546-2548
    • Yang, Z.1    Ma, M.2    Xu, B.3
  • 291
    • 84856168201 scopus 로고    scopus 로고
    • Peptide-based and polypeptide-based hydrogels for drug delivery and tissue engineering
    • In: Deming T, ed., vol. .
    • Altunbas A, Pochan DJ. Peptide-based and polypeptide-based hydrogels for drug delivery and tissue engineering. In: Deming T, ed. Peptide-Based Materials, vol. 310. 2012, 135-167.
    • (2012) Peptide-Based Materials , vol.310 , pp. 135-167
    • Altunbas, A.1    Pochan, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.