메뉴 건너뛰기




Volumn 32, Issue 18, 2011, Pages 4198-4204

Evolving the use of peptides as components of biomaterials

Author keywords

Biomaterials; Extracellular matrix; Peptide; Regenerative medicine; Tissue engineering

Indexed keywords

CELL BEHAVIORS; DE NOVO DESIGN; DEVELOPMENT PROGRAMS; EXTRACELLULAR MATRIX; NON-NATIVE; PEPTIDE LIGAND; REGENERATIVE MEDICINE;

EID: 79955095294     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2011.02.030     Document Type: Article
Times cited : (193)

References (102)
  • 1
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis. I. The synthesis of a tetrapeptide
    • Merrifield R.B. Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J Am Chem Soc 1963, 85:2149-2154.
    • (1963) J Am Chem Soc , vol.85 , pp. 2149-2154
    • Merrifield, R.B.1
  • 2
    • 39149116365 scopus 로고    scopus 로고
    • Solid-phase peptide synthesis: from standard procedures to the synthesis of difficult sequences
    • Coin I., Beyermann M., Bienert M. Solid-phase peptide synthesis: from standard procedures to the synthesis of difficult sequences. Nat Protoc 2007, 2:3247-3256.
    • (2007) Nat Protoc , vol.2 , pp. 3247-3256
    • Coin, I.1    Beyermann, M.2    Bienert, M.3
  • 3
    • 0028233684 scopus 로고
    • Some 'difficult sequences' made easy. A study of interchain association in solid-phase peptide synthesis
    • Hyde C., Johnson T., Owen D., Quibell M., Sheppard R.C. Some 'difficult sequences' made easy. A study of interchain association in solid-phase peptide synthesis. Int J Pept Protein Res 1994, 43:431-440.
    • (1994) Int J Pept Protein Res , vol.43 , pp. 431-440
    • Hyde, C.1    Johnson, T.2    Owen, D.3    Quibell, M.4    Sheppard, R.C.5
  • 4
    • 1642458245 scopus 로고    scopus 로고
    • Novel and efficient synthesis of difficult sequence-containing peptides through O-N intramolecular acyl migration reaction of O-acyl isopeptides
    • Sohma Y., Sasaki M., Hayashi Y., Kimura T., Kiso Y. Novel and efficient synthesis of difficult sequence-containing peptides through O-N intramolecular acyl migration reaction of O-acyl isopeptides. Chem Commun (Camb) 2004, 7:124-125.
    • (2004) Chem Commun (Camb) , vol.7 , pp. 124-125
    • Sohma, Y.1    Sasaki, M.2    Hayashi, Y.3    Kimura, T.4    Kiso, Y.5
  • 5
    • 34548596987 scopus 로고    scopus 로고
    • Segment coupling to a highly hindered N-terminal, alamethicin-related alpha-aminoisobutyric acid (Aib) residue
    • Carpino L.A., Abdel-Maksoud A.A., Mansour E.M., Zewail M.A. Segment coupling to a highly hindered N-terminal, alamethicin-related alpha-aminoisobutyric acid (Aib) residue. Tetrahedron Lett 2007, 48:7404-7407.
    • (2007) Tetrahedron Lett , vol.48 , pp. 7404-7407
    • Carpino, L.A.1    Abdel-Maksoud, A.A.2    Mansour, E.M.3    Zewail, M.A.4
  • 6
    • 0028994059 scopus 로고
    • Pseudo-prolines (psi Pro) for accessing "inaccessible" peptides
    • Mutter M., Nefzi A., Sato T., Sun X., Wahl F., Wohr T. Pseudo-prolines (psi Pro) for accessing "inaccessible" peptides. Pept Res 1995, 8:145-153.
    • (1995) Pept Res , vol.8 , pp. 145-153
    • Mutter, M.1    Nefzi, A.2    Sato, T.3    Sun, X.4    Wahl, F.5    Wohr, T.6
  • 7
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher M.D., Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 1984, 309:30-33.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 8
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu Rev Cell Dev Biol 1996, 12:697-715.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 9
    • 70349773945 scopus 로고    scopus 로고
    • Emerging concepts in engineering extracellular matrix variants for directing cell phenotype
    • Carson A.E., Barker T.H. Emerging concepts in engineering extracellular matrix variants for directing cell phenotype. Regen Med 2009, 4:593-600.
    • (2009) Regen Med , vol.4 , pp. 593-600
    • Carson, A.E.1    Barker, T.H.2
  • 10
    • 0037965624 scopus 로고    scopus 로고
    • Synthetic matrix metalloproteinase-sensitive hydrogels for the conduction of tissue regeneration: engineering cell-invasion characteristics
    • Lutolf M.P., Lauer-Fields J.L., Schmoekel H.G., Metters A.T., Weber F.E., Fields G.B., et al. Synthetic matrix metalloproteinase-sensitive hydrogels for the conduction of tissue regeneration: engineering cell-invasion characteristics. Proc Natl Acad Sci U S A 2003, 100:5413-5418.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5413-5418
    • Lutolf, M.P.1    Lauer-Fields, J.L.2    Schmoekel, H.G.3    Metters, A.T.4    Weber, F.E.5    Fields, G.B.6
  • 11
    • 79955095317 scopus 로고    scopus 로고
    • SPARC-derived protease substrates to enhance the plasmin sensitivity of molecularly engineered PEG hydrogels. Biomaterials.
    • Patterson J, Hubbell JA. SPARC-derived protease substrates to enhance the plasmin sensitivity of molecularly engineered PEG hydrogels. Biomaterials.
    • Patterson, J.1    Hubbell, J.A.2
  • 12
    • 77955773774 scopus 로고    scopus 로고
    • Enhanced proteolytic degradation of molecularly engineered PEG hydrogels in response to MMP-1 and MMP-2
    • Patterson J., Hubbell J.A. Enhanced proteolytic degradation of molecularly engineered PEG hydrogels in response to MMP-1 and MMP-2. Biomaterials 2010, 31:7836-7845.
    • (2010) Biomaterials , vol.31 , pp. 7836-7845
    • Patterson, J.1    Hubbell, J.A.2
  • 13
    • 54049142842 scopus 로고    scopus 로고
    • Matrix metalloprotease selective peptide substrates cleavage within hydrogel matrices for cancer chemotherapy activation
    • Tauro J.R., Lee B.S., Lateef S.S., Gemeinhart R.A. Matrix metalloprotease selective peptide substrates cleavage within hydrogel matrices for cancer chemotherapy activation. Peptides 2008, 29:1965-1973.
    • (2008) Peptides , vol.29 , pp. 1965-1973
    • Tauro, J.R.1    Lee, B.S.2    Lateef, S.S.3    Gemeinhart, R.A.4
  • 14
    • 77956012698 scopus 로고    scopus 로고
    • Protease degradable tethers for controlled and cell-mediated release of nanoparticles in 2- and 3-dimensions
    • Tokatlian T., Shrum C.T., Kadoya W.M., Segura T. Protease degradable tethers for controlled and cell-mediated release of nanoparticles in 2- and 3-dimensions. Biomaterials 2010, 31:8072-8080.
    • (2010) Biomaterials , vol.31 , pp. 8072-8080
    • Tokatlian, T.1    Shrum, C.T.2    Kadoya, W.M.3    Segura, T.4
  • 15
    • 68949085385 scopus 로고    scopus 로고
    • A surface plasmon resonance-based solution affinity assay for heparan sulfate-binding proteins
    • Cochran S., Li C.P., Ferro V. A surface plasmon resonance-based solution affinity assay for heparan sulfate-binding proteins. Glycoconj J 2009, 26:577-587.
    • (2009) Glycoconj J , vol.26 , pp. 577-587
    • Cochran, S.1    Li, C.P.2    Ferro, V.3
  • 16
    • 1042278145 scopus 로고    scopus 로고
    • Fibronectin binds insulin-like growth factor-binding protein 5 and abolishes Its ligand-dependent action on cell migration
    • Xu Q., Yan B., Li S., Duan C. Fibronectin binds insulin-like growth factor-binding protein 5 and abolishes Its ligand-dependent action on cell migration. J Biol Chem 2004, 279:4269-4277.
    • (2004) J Biol Chem , vol.279 , pp. 4269-4277
    • Xu, Q.1    Yan, B.2    Li, S.3    Duan, C.4
  • 17
    • 25444495268 scopus 로고    scopus 로고
    • Novel hepatocyte growth factor (HGF) binding domains on fibronectin and vitronectin coordinate a distinct and amplified Met-integrin induced signalling pathway in endothelial cells
    • Rahman S., Patel Y., Murray J., Patel K.V., Sumathipala R., Sobel M., et al. Novel hepatocyte growth factor (HGF) binding domains on fibronectin and vitronectin coordinate a distinct and amplified Met-integrin induced signalling pathway in endothelial cells. BMC Cell Biol 2005, 6:8.
    • (2005) BMC Cell Biol , vol.6 , pp. 8
    • Rahman, S.1    Patel, Y.2    Murray, J.3    Patel, K.V.4    Sumathipala, R.5    Sobel, M.6
  • 18
    • 32344444422 scopus 로고    scopus 로고
    • CT domain of CCN2/CTGF directly interacts with fibronectin and enhances cell adhesion of chondrocytes through integrin alpha5beta1
    • Hoshijima M., Hattori T., Inoue M., Araki D., Hanagata H., Miyauchi A., et al. CT domain of CCN2/CTGF directly interacts with fibronectin and enhances cell adhesion of chondrocytes through integrin alpha5beta1. FEBS Lett 2006, 580:1376-1382.
    • (2006) FEBS Lett , vol.580 , pp. 1376-1382
    • Hoshijima, M.1    Hattori, T.2    Inoue, M.3    Araki, D.4    Hanagata, H.5    Miyauchi, A.6
  • 19
    • 78649727712 scopus 로고    scopus 로고
    • The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain
    • Martino M.M., Hubbell J.A. The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain. FASEB J 2010, 24:4711-4721.
    • (2010) FASEB J , vol.24 , pp. 4711-4721
    • Martino, M.M.1    Hubbell, J.A.2
  • 20
    • 77149150968 scopus 로고    scopus 로고
    • Anchorage of VEGF to the extracellular matrix conveys differential signaling responses to endothelial cells
    • Chen T.T., Luque A., Lee S., Anderson S.M., Segura T., Iruela-Arispe M.L. Anchorage of VEGF to the extracellular matrix conveys differential signaling responses to endothelial cells. J Cell Biol 2010, 188:595-609.
    • (2010) J Cell Biol , vol.188 , pp. 595-609
    • Chen, T.T.1    Luque, A.2    Lee, S.3    Anderson, S.M.4    Segura, T.5    Iruela-Arispe, M.L.6
  • 21
    • 33644804663 scopus 로고    scopus 로고
    • Discovery of a sulfated tetrapeptide that binds to vascular endothelial growth factor
    • Maynard H.D., Hubbell J.A. Discovery of a sulfated tetrapeptide that binds to vascular endothelial growth factor. Acta Biomater 2005, 1:451-459.
    • (2005) Acta Biomater , vol.1 , pp. 451-459
    • Maynard, H.D.1    Hubbell, J.A.2
  • 22
    • 35349029811 scopus 로고    scopus 로고
    • Heparin-mimetic sulfated peptides with modulated affinities for heparin-binding peptides and growth factors
    • Kim S.H., Kiick K.L. Heparin-mimetic sulfated peptides with modulated affinities for heparin-binding peptides and growth factors. Peptides 2007, 28:2125-2136.
    • (2007) Peptides , vol.28 , pp. 2125-2136
    • Kim, S.H.1    Kiick, K.L.2
  • 23
    • 10644264493 scopus 로고    scopus 로고
    • The effect of functionalized self-assembling peptide scaffolds on human aortic endothelial cell function
    • Genove E., Shen C., Zhang S., Semino C.E. The effect of functionalized self-assembling peptide scaffolds on human aortic endothelial cell function. Biomaterials 2005, 26:3341-3351.
    • (2005) Biomaterials , vol.26 , pp. 3341-3351
    • Genove, E.1    Shen, C.2    Zhang, S.3    Semino, C.E.4
  • 24
    • 36249032275 scopus 로고    scopus 로고
    • Biological designer self-assembling peptide nanofiber scaffolds significantly enhance osteoblast proliferation, differentiation and 3-D migration
    • Horii A., Wang X., Gelain F., Zhang S. Biological designer self-assembling peptide nanofiber scaffolds significantly enhance osteoblast proliferation, differentiation and 3-D migration. PLoS One 2007, 2:e190.
    • (2007) PLoS One , vol.2
    • Horii, A.1    Wang, X.2    Gelain, F.3    Zhang, S.4
  • 25
    • 0027416047 scopus 로고
    • Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane
    • Zhang S., Holmes T., Lockshin C., Rich A. Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane. Proc Natl Acad Sci U S A 1993, 90:3334-3338.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3334-3338
    • Zhang, S.1    Holmes, T.2    Lockshin, C.3    Rich, A.4
  • 26
    • 40049102344 scopus 로고    scopus 로고
    • Modulating the mechanical properties of self-assembled peptide hydrogels via native chemical ligation
    • Jung J.P., Jones J.L., Cronier S.A., Collier J.H. Modulating the mechanical properties of self-assembled peptide hydrogels via native chemical ligation. Biomaterials 2008, 29:2143-2151.
    • (2008) Biomaterials , vol.29 , pp. 2143-2151
    • Jung, J.P.1    Jones, J.L.2    Cronier, S.A.3    Collier, J.H.4
  • 28
    • 77950342360 scopus 로고    scopus 로고
    • Self-assembly of peptide amphiphiles: from molecules to nanostructures to biomaterials
    • Cui H., Webber M.J., Stupp S.I. Self-assembly of peptide amphiphiles: from molecules to nanostructures to biomaterials. Biopolymers 2010, 94:1-18.
    • (2010) Biopolymers , vol.94 , pp. 1-18
    • Cui, H.1    Webber, M.J.2    Stupp, S.I.3
  • 29
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • Hartgerink J.D., Beniash E., Stupp S.I. 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
  • 30
    • 1442281238 scopus 로고    scopus 로고
    • Selective differentiation of neural progenitor cells by high-epitope density nanofibers
    • Silva G.A., Czeisler C., Niece K.L., Beniash E., Harrington D.A., Kessler J.A., et al. Selective differentiation of neural progenitor cells by high-epitope density nanofibers. Science 2004, 303:1352-1355.
    • (2004) Science , vol.303 , pp. 1352-1355
    • Silva, G.A.1    Czeisler, C.2    Niece, K.L.3    Beniash, E.4    Harrington, D.A.5    Kessler, J.A.6
  • 32
    • 77950352015 scopus 로고    scopus 로고
    • Building fibrous biomaterials from alpha-helical and collagen-like coiled-coil peptides
    • Woolfson D.N. Building fibrous biomaterials from alpha-helical and collagen-like coiled-coil peptides. Biopolymers 2010, 94:118-127.
    • (2010) Biopolymers , vol.94 , pp. 118-127
    • Woolfson, D.N.1
  • 33
    • 77955795393 scopus 로고    scopus 로고
    • More than just bare scaffolds: towards multi-component and decorated fibrous biomaterials
    • Woolfson D.N., Mahmoud Z.N. More than just bare scaffolds: towards multi-component and decorated fibrous biomaterials. Chem Soc Rev 2010, 39:3464-3479.
    • (2010) Chem Soc Rev , vol.39 , pp. 3464-3479
    • Woolfson, D.N.1    Mahmoud, Z.N.2
  • 34
    • 34249943399 scopus 로고    scopus 로고
    • Controlling hydrogelation kinetics by peptide design for three-dimensional encapsulation and injectable delivery of cells
    • Haines-Butterick L., Rajagopal K., Branco M., Salick D., Rughani R., Pilarz M., et al. Controlling hydrogelation kinetics by peptide design for three-dimensional encapsulation and injectable delivery of cells. Proc Natl Acad Sci U S A 2007, 104:7791-7796.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7791-7796
    • Haines-Butterick, L.1    Rajagopal, K.2    Branco, M.3    Salick, D.4    Rughani, R.5    Pilarz, M.6
  • 36
    • 70349173315 scopus 로고    scopus 로고
    • Tuning the pH responsiveness of beta-hairpin peptide folding, self-assembly, and hydrogel material formation
    • Rajagopal K., Lamm M.S., Haines-Butterick L.A., Pochan D.J., Schneider J.P. Tuning the pH responsiveness of beta-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
  • 37
    • 0037132592 scopus 로고    scopus 로고
    • Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide
    • Schneider J.P., Pochan D.J., Ozbas B., Rajagopal K., Pakstis L., Kretsinger J. Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide. J Am Chem Soc 2002, 124:15030-15037.
    • (2002) J Am Chem Soc , vol.124 , pp. 15030-15037
    • Schneider, J.P.1    Pochan, D.J.2    Ozbas, B.3    Rajagopal, K.4    Pakstis, L.5    Kretsinger, J.6
  • 39
    • 60849093458 scopus 로고    scopus 로고
    • Self-assembled peptide-based hydrogels as scaffolds for anchorage-dependent cells
    • Zhou M., Smith A.M., Das A.K., Hodson N.W., Collins R.F., Ulijn R.V., et al. Self-assembled peptide-based hydrogels as scaffolds for anchorage-dependent cells. Biomaterials 2009, 30:2523-2530.
    • (2009) Biomaterials , vol.30 , pp. 2523-2530
    • Zhou, M.1    Smith, A.M.2    Das, A.K.3    Hodson, N.W.4    Collins, R.F.5    Ulijn, R.V.6
  • 40
    • 33644944179 scopus 로고    scopus 로고
    • Using a kinase/phosphatase switch to regulate a supramolecular hydrogel and forming the supramolecular hydrogel in vivo
    • Yang Z., Liang G., Wang L., Xu B. Using a kinase/phosphatase switch to regulate a supramolecular hydrogel and forming the supramolecular hydrogel in vivo. J Am Chem Soc 2006, 128:3038-3043.
    • (2006) J Am Chem Soc , vol.128 , pp. 3038-3043
    • Yang, Z.1    Liang, G.2    Wang, L.3    Xu, B.4
  • 41
    • 40549112983 scopus 로고    scopus 로고
    • Enzymatic hydrogelation of small molecules
    • Yang Z., Liang G., Xu B. Enzymatic hydrogelation of small molecules. Acc Chem Res 2008, 41:315-326.
    • (2008) Acc Chem Res , vol.41 , pp. 315-326
    • Yang, Z.1    Liang, G.2    Xu, B.3
  • 42
    • 77955778279 scopus 로고    scopus 로고
    • Multi-component extracellular matrices based on peptide self-assembly
    • Collier J.H., Rudra J.S., Gasiorowski J.Z., Jung J.P. Multi-component extracellular matrices based on peptide self-assembly. Chem Soc Rev 2010, 39:3413-3424.
    • (2010) Chem Soc Rev , vol.39 , pp. 3413-3424
    • Collier, J.H.1    Rudra, J.S.2    Gasiorowski, J.Z.3    Jung, J.P.4
  • 43
    • 77950350040 scopus 로고    scopus 로고
    • Fibrillar peptide gels in biotechnology and biomedicine
    • Jung J.P., Gasiorowski J.Z., Collier J.H. Fibrillar peptide gels in biotechnology and biomedicine. Biopolymers 2010, 94:49-59.
    • (2010) Biopolymers , vol.94 , pp. 49-59
    • Jung, J.P.1    Gasiorowski, J.Z.2    Collier, J.H.3
  • 44
    • 77953809370 scopus 로고    scopus 로고
    • Bone regeneration mediated by biomimetic mineralization of a nanofiber matrix
    • Mata A., Geng Y., Henrikson K.J., Aparicio C., Stock S.R., Satcher R.L., et al. Bone regeneration mediated by biomimetic mineralization of a nanofiber matrix. Biomaterials 2010, 31:6004-6012.
    • (2010) Biomaterials , vol.31 , pp. 6004-6012
    • Mata, A.1    Geng, Y.2    Henrikson, K.J.3    Aparicio, C.4    Stock, S.R.5    Satcher, R.L.6
  • 47
    • 0037427331 scopus 로고    scopus 로고
    • Mussel adhesive protein mimetic polymers for the preparation of nonfouling surfaces
    • Dalsin J.L., Hu B.H., Lee B.P., Messersmith P.B. Mussel adhesive protein mimetic polymers for the preparation of nonfouling surfaces. J Am Chem Soc 2003, 125:4253-4258.
    • (2003) J Am Chem Soc , vol.125 , pp. 4253-4258
    • Dalsin, J.L.1    Hu, B.H.2    Lee, B.P.3    Messersmith, P.B.4
  • 50
    • 35348945857 scopus 로고    scopus 로고
    • Mussel-inspired surface chemistry for multifunctional coatings
    • Lee H., Dellatore S.M., Miller W.M., Messersmith P.B. Mussel-inspired surface chemistry for multifunctional coatings. Science 2007, 318:426-430.
    • (2007) Science , vol.318 , pp. 426-430
    • Lee, H.1    Dellatore, S.M.2    Miller, W.M.3    Messersmith, P.B.4
  • 51
    • 34548530712 scopus 로고    scopus 로고
    • Selection and analysis of solid-binding peptides
    • Baneyx F., Schwartz D.T. Selection and analysis of solid-binding peptides. Curr Opin Biotechnol 2007, 18:312-317.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 312-317
    • Baneyx, F.1    Schwartz, D.T.2
  • 52
    • 34548814155 scopus 로고    scopus 로고
    • Protein engineering with bacterial display
    • Daugherty P.S. Protein engineering with bacterial display. Curr Opin Struct Biol 2007, 17:474-480.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 474-480
    • Daugherty, P.S.1
  • 53
    • 55049092204 scopus 로고    scopus 로고
    • Immobilization of growth factors on collagen scaffolds mediated by polyanionic collagen mimetic peptides and its effect on endothelial cell morphogenesis
    • Wang A.Y., Leong S., Liang Y.C., Huang R.C., Chen C.S., Yu S.M. Immobilization of growth factors on collagen scaffolds mediated by polyanionic collagen mimetic peptides and its effect on endothelial cell morphogenesis. Biomacromolecules 2008, 9:2929-2936.
    • (2008) Biomacromolecules , vol.9 , pp. 2929-2936
    • Wang, A.Y.1    Leong, S.2    Liang, Y.C.3    Huang, R.C.4    Chen, C.S.5    Yu, S.M.6
  • 54
    • 16244397716 scopus 로고    scopus 로고
    • Facile modification of collagen directed by collagen mimetic peptides
    • Wang A.Y., Mo X., Chen C.S., Yu S.M. Facile modification of collagen directed by collagen mimetic peptides. J Am Chem Soc 2005, 127:4130-4131.
    • (2005) J Am Chem Soc , vol.127 , pp. 4130-4131
    • Wang, A.Y.1    Mo, X.2    Chen, C.S.3    Yu, S.M.4
  • 55
    • 39749198122 scopus 로고    scopus 로고
    • Biofunctional polymer nanoparticles for intra-articular targeting and retention in cartilage
    • Rothenfluh D.A., Bermudez H., O'Neil C.P., Hubbell J.A. Biofunctional polymer nanoparticles for intra-articular targeting and retention in cartilage. Nat Mater 2008, 7:248-254.
    • (2008) Nat Mater , vol.7 , pp. 248-254
    • Rothenfluh, D.A.1    Bermudez, H.2    O'Neil, C.P.3    Hubbell, J.A.4
  • 56
    • 33748456564 scopus 로고    scopus 로고
    • Peptide array-based interaction assay of solid-bound peptides and anchorage-dependant cells and its effectiveness in cell-adhesive peptide design
    • Kato R., Kaga C., Kunimatsu M., Kobayashi T., Honda H. Peptide array-based interaction assay of solid-bound peptides and anchorage-dependant cells and its effectiveness in cell-adhesive peptide design. J Biosci Bioeng 2006, 101:485-495.
    • (2006) J Biosci Bioeng , vol.101 , pp. 485-495
    • Kato, R.1    Kaga, C.2    Kunimatsu, M.3    Kobayashi, T.4    Honda, H.5
  • 57
    • 57449089782 scopus 로고    scopus 로고
    • Identification of peptides with targeted adhesion to bone-like mineral via phage display and computational modeling
    • Segvich S., Biswas S., Becker U., Kohn D.H. Identification of peptides with targeted adhesion to bone-like mineral via phage display and computational modeling. Cells Tissues Organs 2009, 189:245-251.
    • (2009) Cells Tissues Organs , vol.189 , pp. 245-251
    • Segvich, S.1    Biswas, S.2    Becker, U.3    Kohn, D.H.4
  • 58
    • 77951256699 scopus 로고    scopus 로고
    • Peptide aptamers against titanium-based implants identified through phage display
    • Liu Y., Mao J., Zhou B., Wei W., Gong S. Peptide aptamers against titanium-based implants identified through phage display. J Mater Sci Mater Med 2010, 21:1103-1107.
    • (2010) J Mater Sci Mater Med , vol.21 , pp. 1103-1107
    • Liu, Y.1    Mao, J.2    Zhou, B.3    Wei, W.4    Gong, S.5
  • 59
    • 75749118484 scopus 로고    scopus 로고
    • High-throughput discovery of synthetic surfaces that support proliferation of pluripotent cells
    • Derda R., Musah S., Orner B.P., Klim J.R., Li L., Kiessling L.L. High-throughput discovery of synthetic surfaces that support proliferation of pluripotent cells. J Am Chem Soc 2010, 132:1289-1295.
    • (2010) J Am Chem Soc , vol.132 , pp. 1289-1295
    • Derda, R.1    Musah, S.2    Orner, B.P.3    Klim, J.R.4    Li, L.5    Kiessling, L.L.6
  • 60
    • 0037117516 scopus 로고    scopus 로고
    • Selective immobilization of proteins to self-assembled monolayers presenting active site-directed capture ligands
    • Hodneland C.D., Lee Y.S., Min D.H., Mrksich M. Selective immobilization of proteins to self-assembled monolayers presenting active site-directed capture ligands. Proc Natl Acad Sci U S A 2002, 99:5048-5052.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 5048-5052
    • Hodneland, C.D.1    Lee, Y.S.2    Min, D.H.3    Mrksich, M.4
  • 61
    • 74049143907 scopus 로고    scopus 로고
    • Using self-assembled monolayers to model cell adhesion to the 9th and 10th type III domains of fibronectin
    • Eisenberg J.L., Piper J.L., Mrksich M. Using self-assembled monolayers to model cell adhesion to the 9th and 10th type III domains of fibronectin. Langmuir 2009, 25:13942-13951.
    • (2009) Langmuir , vol.25 , pp. 13942-13951
    • Eisenberg, J.L.1    Piper, J.L.2    Mrksich, M.3
  • 63
    • 0034888333 scopus 로고    scopus 로고
    • Conjugate addition reactions combined with free-radical cross-linking for the design of materials for tissue engineering
    • Elbert D.L., Hubbell J.A. Conjugate addition reactions combined with free-radical cross-linking for the design of materials for tissue engineering. Biomacromolecules 2001, 2:430-441.
    • (2001) Biomacromolecules , vol.2 , pp. 430-441
    • Elbert, D.L.1    Hubbell, J.A.2
  • 65
    • 0035210936 scopus 로고    scopus 로고
    • Systematic modulation of Michael-type reactivity of thiols through the use of charged amino acids
    • Lutolf M.P., Tirelli N., Cerritelli S., Cavalli L., Hubbell J.A. Systematic modulation of Michael-type reactivity of thiols through the use of charged amino acids. Bioconjug Chem 2001, 12:1051-1056.
    • (2001) Bioconjug Chem , vol.12 , pp. 1051-1056
    • Lutolf, M.P.1    Tirelli, N.2    Cerritelli, S.3    Cavalli, L.4    Hubbell, J.A.5
  • 66
    • 64549130908 scopus 로고    scopus 로고
    • Sequential crosslinking to control cellular spreading in 3-dimensional hydrogels
    • Khetan S., Katz J.S., Burdick J.A. Sequential crosslinking to control cellular spreading in 3-dimensional hydrogels. Soft Matter 2009, 5:1601-1606.
    • (2009) Soft Matter , vol.5 , pp. 1601-1606
    • Khetan, S.1    Katz, J.S.2    Burdick, J.A.3
  • 67
    • 0032941232 scopus 로고    scopus 로고
    • Alginate hydrogels as synthetic extracellular matrix materials
    • Rowley J.A., Madlambayan G., Mooney D.J. Alginate hydrogels as synthetic extracellular matrix materials. Biomaterials 1999, 20:45-53.
    • (1999) Biomaterials , vol.20 , pp. 45-53
    • Rowley, J.A.1    Madlambayan, G.2    Mooney, D.J.3
  • 68
    • 43449108552 scopus 로고    scopus 로고
    • Efficient construction of therapeutics, bioconjugates, biomaterials and bioactive surfaces using azide-alkyne "click" chemistry
    • Lutz J.F., Zarafshani Z. Efficient construction of therapeutics, bioconjugates, biomaterials and bioactive surfaces using azide-alkyne "click" chemistry. Adv Drug Delivery Reviews 2008, 60:958-970.
    • (2008) Adv Drug Delivery Reviews , vol.60 , pp. 958-970
    • Lutz, J.F.1    Zarafshani, Z.2
  • 69
    • 19744370243 scopus 로고    scopus 로고
    • PEG- and peptide-grafted aliphatic polyesters by click chemistry
    • Parrish B., Breitenkamp R.B., Emrick T. PEG- and peptide-grafted aliphatic polyesters by click chemistry. J Am Chem Soc 2005, 127:7404-7410.
    • (2005) J Am Chem Soc , vol.127 , pp. 7404-7410
    • Parrish, B.1    Breitenkamp, R.B.2    Emrick, T.3
  • 70
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson P.E., Muir T.W., Clark-Lewis I., Kent S.B. Synthesis of proteins by native chemical ligation. Science 1994, 266:776-779.
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.4
  • 71
    • 68849104748 scopus 로고    scopus 로고
    • Hydrogels cross-linked by native chemical ligation
    • Hu B.H., Su J., Messersmith P.B. Hydrogels cross-linked by native chemical ligation. Biomacromolecules 2009, 10:2194-2200.
    • (2009) Biomacromolecules , vol.10 , pp. 2194-2200
    • Hu, B.H.1    Su, J.2    Messersmith, P.B.3
  • 72
    • 25144516630 scopus 로고    scopus 로고
    • Synthesis of collagen-like peptide polymers by native chemical ligation
    • Paramonov S.E., Gauba V., Hartgerink J.D. Synthesis of collagen-like peptide polymers by native chemical ligation. Macromolecules 2005, 38:7555-7561.
    • (2005) Macromolecules , vol.38 , pp. 7555-7561
    • Paramonov, S.E.1    Gauba, V.2    Hartgerink, J.D.3
  • 73
    • 77950363627 scopus 로고    scopus 로고
    • Chemoselective ligation techniques: modern applications of time-honored chemistry
    • Tiefenbrunn T.K., Dawson P.E. Chemoselective ligation techniques: modern applications of time-honored chemistry. Biopolymers 2010, 94:95-106.
    • (2010) Biopolymers , vol.94 , pp. 95-106
    • Tiefenbrunn, T.K.1    Dawson, P.E.2
  • 74
    • 62449282062 scopus 로고    scopus 로고
    • Total chemical synthesis of proteins
    • Kent S.B. Total chemical synthesis of proteins. Chem Soc Reviews 2009, 38:338-351.
    • (2009) Chem Soc Reviews , vol.38 , pp. 338-351
    • Kent, S.B.1
  • 75
    • 34248230589 scopus 로고    scopus 로고
    • Convergent chemical synthesis and crystal structure of a 203 amino acid "covalent dimer" HIV-1 protease enzyme molecule
    • Torbeev V.Y., Kent S.B. Convergent chemical synthesis and crystal structure of a 203 amino acid "covalent dimer" HIV-1 protease enzyme molecule. Angew Chem International Ed 2007, 46:1667-1670.
    • (2007) Angew Chem International Ed , vol.46 , pp. 1667-1670
    • Torbeev, V.Y.1    Kent, S.B.2
  • 76
    • 65649099741 scopus 로고    scopus 로고
    • Chemical synthesis and biotinylation of the thrombospondin domain TSR2
    • Tiefenbrunn T.K., Dawson P.E. Chemical synthesis and biotinylation of the thrombospondin domain TSR2. Protein Sci 2009, 18:970-979.
    • (2009) Protein Sci , vol.18 , pp. 970-979
    • Tiefenbrunn, T.K.1    Dawson, P.E.2
  • 77
    • 77951689718 scopus 로고    scopus 로고
    • Immobilization of peptides with distinct biological activities onto stem cell culture substrates using orthogonal chemistries
    • Hudalla G.A., Murphy W.L. Immobilization of peptides with distinct biological activities onto stem cell culture substrates using orthogonal chemistries. Langmuir 2010, 26:6449-6456.
    • (2010) Langmuir , vol.26 , pp. 6449-6456
    • Hudalla, G.A.1    Murphy, W.L.2
  • 78
    • 34248138480 scopus 로고    scopus 로고
    • Site-specific protein immobilization through N-terminal oxime linkages
    • Christman K.L., Broyer R.M., Tolstyka Z.P., Maynard H.D. Site-specific protein immobilization through N-terminal oxime linkages. J Mater Chem 2007, 17:2021-2027.
    • (2007) J Mater Chem , vol.17 , pp. 2021-2027
    • Christman, K.L.1    Broyer, R.M.2    Tolstyka, Z.P.3    Maynard, H.D.4
  • 79
    • 34548293043 scopus 로고    scopus 로고
    • Functional modification of biodegradable polyesters through a chemoselective approach: application to biomaterial surfaces
    • Taniguchi I., Kuhlman W.A., Mayes A.M., Griffith L.G. Functional modification of biodegradable polyesters through a chemoselective approach: application to biomaterial surfaces. Polym Int 2006, 55:1385-1397.
    • (2006) Polym Int , vol.55 , pp. 1385-1397
    • Taniguchi, I.1    Kuhlman, W.A.2    Mayes, A.M.3    Griffith, L.G.4
  • 80
    • 78049256803 scopus 로고    scopus 로고
    • In situ growth of a PEG-like polymer from the C terminus of an intein fusion protein improves pharmacokinetics and tumor accumulation
    • Proceedings of the National Academy of Sciences of the United States of America
    • Gao W, Liu W, Christensen T, Zalutsky MR, Chilkoti A. In situ growth of a PEG-like polymer from the C terminus of an intein fusion protein improves pharmacokinetics and tumor accumulation. Proceedings of the National Academy of Sciences of the United States of America;107:16432-16437.
    • , vol.107 , pp. 16432-16437
    • Gao, W.1    Liu, W.2    Christensen, T.3    Zalutsky, M.R.4    Chilkoti, A.5
  • 81
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • Muir T.W. Semisynthesis of proteins by expressed protein ligation. Annu review Biochemistry 2003, 72:249-289.
    • (2003) Annu review Biochemistry , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 82
    • 0040559903 scopus 로고    scopus 로고
    • The cyclization and polymerization of bacterially expressed proteins using modified self-splicing inteins
    • Evans T.C., Benner J., Xu M.Q. The cyclization and polymerization of bacterially expressed proteins using modified self-splicing inteins. J Biological Chemistry 1999, 274:18359-18363.
    • (1999) J Biological Chemistry , vol.274 , pp. 18359-18363
    • Evans, T.C.1    Benner, J.2    Xu, M.Q.3
  • 83
    • 70349292246 scopus 로고    scopus 로고
    • Rational design of peptide-based building blocks for nanoscience and synthetic biology
    • discussion 359-372
    • Armstrong C.T., Boyle A.L., Bromley E.H., Mahmoud Z.N., Smith L., Thomson A.R., et al. Rational design of peptide-based building blocks for nanoscience and synthetic biology. Faraday Discuss 2009, 143:305-317. discussion 359-372.
    • (2009) Faraday Discuss , vol.143 , pp. 305-317
    • Armstrong, C.T.1    Boyle, A.L.2    Bromley, E.H.3    Mahmoud, Z.N.4    Smith, L.5    Thomson, A.R.6
  • 84
  • 85
    • 43549102692 scopus 로고    scopus 로고
    • Alternative binding proteins: biological activity and therapeutic potential of cystine-knot miniproteins
    • Kolmar H. Alternative binding proteins: biological activity and therapeutic potential of cystine-knot miniproteins. Febs J 2008, 275:2684-2690.
    • (2008) Febs J , vol.275 , pp. 2684-2690
    • Kolmar, H.1
  • 86
    • 70349583511 scopus 로고    scopus 로고
    • Discovery, structure and biological activities of cyclotides
    • Daly N.L., Rosengren K.J., Craik D.J. Discovery, structure and biological activities of cyclotides. Adv Drug Deliv Rev 2009, 61:918-930.
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 918-930
    • Daly, N.L.1    Rosengren, K.J.2    Craik, D.J.3
  • 87
    • 70349462873 scopus 로고    scopus 로고
    • Engineered cystine knot peptides that bind alphavbeta3, alphavbeta5, and alpha5beta1 integrins with low-nanomolar affinity
    • Kimura R.H., Levin A.M., Cochran F.V., Cochran J.R. Engineered cystine knot peptides that bind alphavbeta3, alphavbeta5, and alpha5beta1 integrins with low-nanomolar affinity. Proteins 2009, 77:359-369.
    • (2009) Proteins , vol.77 , pp. 359-369
    • Kimura, R.H.1    Levin, A.M.2    Cochran, F.V.3    Cochran, J.R.4
  • 88
    • 77949418669 scopus 로고    scopus 로고
    • Self-assembling multidomain peptide hydrogels: designed susceptibility to enzymatic cleavage allows enhanced cell migration and spreading
    • Galler K.M., Aulisa L., Regan K.R., D'Souza R.N., Hartgerink J.D. Self-assembling multidomain peptide hydrogels: designed susceptibility to enzymatic cleavage allows enhanced cell migration and spreading. J Am Chem Soc 2010, 132:3217-3223.
    • (2010) J Am Chem Soc , vol.132 , pp. 3217-3223
    • Galler, K.M.1    Aulisa, L.2    Regan, K.R.3    D'Souza, R.N.4    Hartgerink, J.D.5
  • 89
    • 70349165421 scopus 로고    scopus 로고
    • Self-assembly of multidomain peptides: sequence variation allows control over cross-linking and viscoelasticity
    • Aulisa L., Dong H., Hartgerink J.D. 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
  • 90
    • 77955795080 scopus 로고    scopus 로고
    • Synthetic collagen mimics: self-assembly of homotrimers, heterotrimers and higher order structures
    • Fallas J.A., O'Leary L.E., Hartgerink J.D. Synthetic collagen mimics: self-assembly of homotrimers, heterotrimers and higher order structures. Chem Soc Rev 2010, 39:3510-3527.
    • (2010) Chem Soc Rev , vol.39 , pp. 3510-3527
    • Fallas, J.A.1    O'Leary, L.E.2    Hartgerink, J.D.3
  • 91
    • 0025880146 scopus 로고
    • Arg-Gly-Asp constrained within cyclic pentapeptides. Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1
    • Aumailley M., Gurrath M., Muller G., Calvete J., Timpl R., Kessler H. Arg-Gly-Asp constrained within cyclic pentapeptides. Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1. FEBS Lett 1991, 291:50-54.
    • (1991) FEBS Lett , vol.291 , pp. 50-54
    • Aumailley, M.1    Gurrath, M.2    Muller, G.3    Calvete, J.4    Timpl, R.5    Kessler, H.6
  • 92
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov R., Yamada K.M. Fibronectin at a glance. J Cell Sci 2002, 115:3861-3863.
    • (2002) J Cell Sci , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 93
    • 0034697649 scopus 로고    scopus 로고
    • An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of peptides
    • Schafmeister C.E., Po J., Verdine G.L. An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of peptides. J Am Chem Soc 2000, 122:5891-5892.
    • (2000) J Am Chem Soc , vol.122 , pp. 5891-5892
    • Schafmeister, C.E.1    Po, J.2    Verdine, G.L.3
  • 95
    • 77956294635 scopus 로고    scopus 로고
    • Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic
    • Bird G.H., Madani N., Perry A.F., Princiotto A.M., Supko J.G., He X., et al. Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic. Proc Natl Acad Sci U S A 2010, 107:14093-14098.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 14093-14098
    • Bird, G.H.1    Madani, N.2    Perry, A.F.3    Princiotto, A.M.4    Supko, J.G.5    He, X.6
  • 99
    • 79952517440 scopus 로고    scopus 로고
    • Multifactorial optimization of endothelial cell growth using modular synthetic extracellular matrices
    • in press, doi:10.1039/C0IB00112K
    • Jung JP, Moyano JV, and Collier JH, " Multifactorial optimization of endothelial cell growth using modular synthetic extracellular matrices" , Integr Biol, 2011, in press, doi:10.1039/C0IB00112K.
    • (2011) Integr Biol
    • Jung, J.P.1    Moyano, J.V.2    Collier, J.H.3
  • 100
    • 66149113351 scopus 로고    scopus 로고
    • Hybrid multicomponent hydrogels for tissue engineering
    • Jia X., Kiick K.L. 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
  • 102
    • 0008926519 scopus 로고    scopus 로고
    • Inhibition of platelet glycoprotein IIb/IIIa with eptifibatide in patients with acute coronary syndromes
    • Topol E., Califf R., Simoons M., Diaz R., Paolasso E., Klein W., et al. Inhibition of platelet glycoprotein IIb/IIIa with eptifibatide in patients with acute coronary syndromes. N Engl J Med 1998, 339:436-443.
    • (1998) N Engl J Med , vol.339 , pp. 436-443
    • Topol, E.1    Califf, R.2    Simoons, M.3    Diaz, R.4    Paolasso, E.5    Klein, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.