메뉴 건너뛰기




Volumn 8, Issue 5, 2013, Pages 823-847

Biomimetic self-assembling peptides as scaffolds for soft tissue engineering

Author keywords

coiled coil; extracellular matrix; fiber; hydrogel; nanostructure; peptide; scaffold; self assembly; tissue engineering; sheet

Indexed keywords

AMPHOPHILE; ARGINYLGLYCYLASPARTIC ACID; BIOMATERIAL; BIOMIMETIC MATERIAL; CHITOSAN; COLLAGEN; COLLAGEN TYPE 1; COLLAGEN TYPE 4; GLYCOSAMINOGLYCAN; LAMININ; MONOMER; NANOPARTICLE; NATURAL PRODUCT; PEPTIDE; POLYACRYLIC ACID; POLYCAPROLACTONE; POLYLACTIC ACID; POLYMER; SILK; TISSUE SCAFFOLD;

EID: 84877675234     PISSN: 17435889     EISSN: 17486963     Source Type: Journal    
DOI: 10.2217/nnm.13.65     Document Type: Review
Times cited : (113)

References (138)
  • 1
    • 0027595948 scopus 로고
    • Tissue engineering
    • Langer R, Vacanti JP. Tissue engineering. Science 260(5110), 920-926 (1993).
    • (1993) Science , vol.260 , Issue.5110 , pp. 920-926
    • Langer, R.1    Vacanti, J.P.2
  • 3
    • 77956434412 scopus 로고    scopus 로고
    • Nanotechnology in drug delivery and tissue engineering: From discovery to applications
    • Shi JJ, Votruba AR, Farokhzad OC, Langer R. Nanotechnology in drug delivery and tissue engineering: from discovery to applications. Nano Lett. 10(9), 3223-3230 (2010).
    • (2010) Nano Lett , vol.10 , Issue.9 , pp. 3223-3230
    • Shi, J.J.1    Votruba, A.R.2    Farokhzad, O.C.3    Langer, R.4
  • 4
    • 55749100987 scopus 로고    scopus 로고
    • Nanotechnology and nanomaterials: Promises for improved tissue regeneration
    • Zhang LJ, Webster TJ. Nanotechnology and nanomaterials: promises for improved tissue regeneration. Nano Today 4(1), 66-80 (2009).
    • (2009) Nano Today , vol.4 , Issue.1 , pp. 66-80
    • Zhang, L.J.1    Webster, T.J.2
  • 6
    • 0032404328 scopus 로고    scopus 로고
    • Development of biocompatible synthetic extracellular matrices for tissue engineering
    • Kim BS, Mooney DJ. Development of biocompatible synthetic extracellular matrices for tissue engineering. Trends Biotechnol. 16(5), 224-230 (1998).
    • (1998) Trends Biotechnol , vol.16 , Issue.5 , pp. 224-230
    • Kim, B.S.1    Mooney, D.J.2
  • 7
    • 37049029660 scopus 로고    scopus 로고
    • Biomimetic materials for tissue engineering
    • Ma PX. Biomimetic materials for tissue engineering. Adv. Drug Del. Rev. 60(2), 184-198 (2008).
    • (2008) Adv. Drug Del. Rev , vol.60 , Issue.2 , pp. 184-198
    • Ma, P.X.1
  • 8
    • 0035054981 scopus 로고    scopus 로고
    • Scaffold design and fabrication technologies for engineering tissues - State of the art and future perspectives
    • Hutmacher DW. Scaffold design and fabrication technologies for engineering tissues - state of the art and future perspectives. J. Biomater. Sci. Polym. Ed. 12(1), 107-124 (2001).
    • (2001) J. Biomater. Sci. Polym. Ed , vol.12 , Issue.1 , pp. 107-124
    • Hutmacher, D.W.1
  • 9
    • 44949166671 scopus 로고    scopus 로고
    • Three-dimensional cell culture matrices: State of the art
    • Lee J, Cuddihy MJ, Kotov NA. Three-dimensional cell culture matrices: state of the art. Tissue Eng. Part B Rev. 14(1), 61-86 (2008).
    • (2008) Tissue Eng. Part B Rev , vol.14 , Issue.1 , pp. 61-86
    • Lee, J.1    Cuddihy, M.J.2    Kotov, N.A.3
  • 10
    • 67650169752 scopus 로고    scopus 로고
    • Hydrogels as extracellular matrix mimics for 3D cell culture
    • Tibbitt MW, Anseth KS. Hydrogels as extracellular matrix mimics for 3D cell culture. Biotechnol. Bioeng. 103(4), 655-663 (2009).
    • (2009) Biotechnol. Bioeng , vol.103 , Issue.4 , pp. 655-663
    • Tibbitt, M.W.1    Anseth, K.S.2
  • 11
    • 0035671158 scopus 로고    scopus 로고
    • The design of scaffolds for use in tissue engineering. Part I. Traditional factors
    • Yang S, Leong K-F, Du Z, Chua C-K. The design of scaffolds for use in tissue engineering. Part I. Traditional factors. Tissue Eng. 7(6), 679-689 (2001).
    • (2001) Tissue Eng , vol.7 , Issue.6 , pp. 679-689
    • Yang, S.1    Leong, K.-F.2    Du, Z.3    Chua, C.-K.4
  • 12
    • 0036139571 scopus 로고    scopus 로고
    • Novel peptide-based biomaterial scaffolds for tissue engineering
    • Holmes TC. Novel peptide-based biomaterial scaffolds for tissue engineering. Trends Biotechnol. 20(1), 16-21 (2002).
    • (2002) Trends Biotechnol , vol.20 , Issue.1 , pp. 16-21
    • Holmes, T.C.1
  • 13
    • 33646595949 scopus 로고    scopus 로고
    • Development and characterization of an acellular human pericardial matrix for tissue engineering
    • Mirsadraee S, Wilcox HE, Korossis SA et al. Development and characterization of an acellular human pericardial matrix for tissue engineering. Tissue Eng. 12(4), 763-773 (2006).
    • (2006) Tissue Eng , vol.12 , Issue.4 , pp. 763-773
    • Mirsadraee, S.1    Wilcox, H.E.2    Korossis, S.A.3
  • 14
    • 24344473397 scopus 로고    scopus 로고
    • In vitro assessment of the functional performance of the decellularized intact porcine aortic root
    • Korossis SA, Wilcox HE, Watterson KG et al. In vitro assessment of the functional performance of the decellularized intact porcine aortic root. J. Heart Valve Dis. 14(3), 408-421 (2005).
    • (2005) J. Heart Valve Dis , vol.14 , Issue.3 , pp. 408-421
    • Korossis, S.A.1    Wilcox, H.E.2    Watterson, K.G.3
  • 15
    • 42049103620 scopus 로고    scopus 로고
    • Development and characterization of an acellular porcine medial meniscus for use in tissue engineering
    • Stapleton TW, Ingram J, Katta J et al. Development and characterization of an acellular porcine medial meniscus for use in tissue engineering. Tissue Eng. Part A 14(4), 505-518 (2008).
    • (2008) Tissue Eng. Part A , vol.14 , Issue.4 , pp. 505-518
    • Stapleton, T.W.1    Ingram, J.2    Katta, J.3
  • 16
    • 1942516513 scopus 로고    scopus 로고
    • Scaffolds for tissue fabrication
    • Ma PX. Scaffolds for tissue fabrication. Mater. Today 7(5), 30-40 (2004).
    • (2004) Mater. Today , vol.7 , Issue.5 , pp. 30-40
    • Ma, P.X.1
  • 17
    • 0026433721 scopus 로고
    • Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures
    • Whitesides GM, Mathias JP, Seto CT. Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures. Science 254(5036), 1312-1319 (1991).
    • (1991) Science , vol.254 , Issue.5036 , pp. 1312-1319
    • Whitesides, G.M.1    Mathias, J.P.2    Seto, C.T.3
  • 18
    • 9444231571 scopus 로고    scopus 로고
    • Engineered and designed peptide-based fibrous biomaterials
    • MacPhee CE, Woolfson DN. Engineered and designed peptide-based fibrous biomaterials. Curr. Opin. Solid State Mater. Sci. 8(2), 141-149 (2004).
    • (2004) Curr. Opin. Solid State Mater. Sci , vol.8 , Issue.2 , pp. 141-149
    • Macphee, C.E.1    Woolfson, D.N.2
  • 19
    • 84862941358 scopus 로고    scopus 로고
    • Peptide synthesis and self-assembly
    • Deming T (Ed.). Springer, Berlin Heidelberg, Germany
    • Maude S, Tai LR, Davies RPW et al. Peptide synthesis and self-assembly. In: Peptide-Based Materials. Deming T (Ed.). Springer, Berlin Heidelberg, Germany, 27-69 (2012).
    • (2012) Peptide-Based Materials , pp. 27-69
    • Maude, S.1    Tai, L.R.2    Rpw, D.3
  • 20
    • 0029064713 scopus 로고
    • Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides
    • Xiong H, Buckwalter BL, Shieh H-M, Hecht MH. Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides. Proc. Natl Acad. Sci. USA 92(14), 6349-6353 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , Issue.14 , pp. 6349-6353
    • Xiong, H.1    Buckwalter, B.L.2    Shieh, H.-M.3    Hecht, M.H.4
  • 21
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM. Protein misfolding, evolution and disease. Trends Biochem. Sci 24(9), 329-332 (1999).
    • (1999) Trends Biochem. Sci , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 22
    • 0028567868 scopus 로고
    • De novo design of b-sheet proteins
    • Hecht MH. De novo design of b-sheet proteins. Proc. Natl Acad. Sci. USA 91(19), 8729-8730 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , Issue.19 , pp. 8729-8730
    • Hecht, M.H.1
  • 23
    • 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. USA 90(8), 3334-3338 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , Issue.8 , pp. 3334-3338
    • Zhang, S.1    Holmes, T.2    Lockshin, C.3    Rich, A.4
  • 24
    • 0034612266 scopus 로고    scopus 로고
    • Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds
    • Holmes TC, De Lacalle S, Su X et al. Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds. Proc. Natl Acad. Sci. USA 97(12), 6728-6733 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , Issue.12 , pp. 6728-6733
    • Holmes, T.C.1    De Lacalle, S.2    Su, X.3
  • 25
    • 0029411957 scopus 로고
    • Self-complementary oligopeptide matrices support mammalian cell attachment
    • Zhang S, Holmes TC, DiPersio CM et al. Self-complementary oligopeptide matrices support mammalian cell attachment. Biomaterials 16(18), 1385-1393 (1995).
    • (1995) Biomaterials , vol.16 , Issue.18 , pp. 1385-1393
    • Zhang, S.1    Holmes, T.C.2    Dipersio, C.M.3
  • 26
    • 39649085356 scopus 로고    scopus 로고
    • Temperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA16-1
    • Ye ZY, Zhang HY, Luo HL et al. Temperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA16-1. J. Pept. Sci. 14(2), 152-162 (2008).
    • (2008) J. Pept. Sci. , vol.14 , Issue.2 , pp. 152-162
    • Ye, Z.Y.1    Zhang, H.Y.2    Luo, H.L.3
  • 27
    • 84877658533 scopus 로고    scopus 로고
    • BD™ PuraMatrix™ Peptide Hydrogel, guidelines for use
    • BD™ PuraMatrix™ Peptide Hydrogel, guidelines for use. BD Biosciences, MA, USA (2004).
    • (2004) BD Biosciences, MA, USA
  • 28
    • 67650679312 scopus 로고    scopus 로고
    • Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model
    • Westermark P, Lundmark K, Westermark GT. Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model. PLoS ONE 4(6), e6041 (2009).
    • (2009) PLoS ONE , vol.4 , Issue.6
    • Westermark, P.1    Lundmark, K.2    Westermark, G.T.3
  • 29
    • 56049106833 scopus 로고    scopus 로고
    • Designer functionalized self-assembling peptide nanofiber scaffolds for growth, migration, and tubulogenesis of human umbilical vein endothelial cells
    • Wang X, Horii A, Zhang S. Designer functionalized self-assembling peptide nanofiber scaffolds for growth, migration, and tubulogenesis of human umbilical vein endothelial cells. Soft Matter 4(12), 2388-2395 (2008).
    • (2008) Soft Matter , vol.4 , Issue.12 , pp. 2388-2395
    • Wang, X.1    Horii, A.2    Zhang, S.3
  • 30
    • 14844338457 scopus 로고    scopus 로고
    • Self-assembling short oligopeptides and the promotion of angiogenesis
    • Narmoneva DA, Oni O, Sieminski AL et al. Self-assembling short oligopeptides and the promotion of angiogenesis. Biomaterials 26(23), 4837-4846 (2005).
    • (2005) Biomaterials , vol.26 , Issue.23 , pp. 4837-4846
    • Narmoneva, D.A.1    Oni, O.2    Sieminski, A.L.3
  • 31
    • 33645504776 scopus 로고    scopus 로고
    • Nano neuro knitting: Peptide nanofiber scaffold for brain repair and axon regeneration with functional return of vision
    • Ellis-Behnke RG, Liang YX, You SW et al. Nano neuro knitting: peptide nanofiber scaffold for brain repair and axon regeneration with functional return of vision. Proc. Natl Acad. Sci. USA 103(13), 5054-5059 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , Issue.13 , pp. 5054-5059
    • Ellis-Behnke, R.G.1    Liang, Y.X.2    You, S.W.3
  • 32
    • 69249227406 scopus 로고    scopus 로고
    • Self-assembling peptide nanofiber scaffold promotes the reconstruction of acutely injured brain
    • Guo J, Leung KKG, Su H et al. Self-assembling peptide nanofiber scaffold promotes the reconstruction of acutely injured brain. Nanomedicine 5(3), 345-351 (2009).
    • (2009) Nanomedicine , vol.5 , Issue.3 , pp. 345-351
    • Guo, J.1    Kkg, L.2    Su, H.3
  • 33
    • 13444283515 scopus 로고    scopus 로고
    • Injectable self-assembling peptide nanofibers create intramyocardial microenvironments for endothelial cells
    • Davis ME, Motion JP, Narmoneva DA et al. Injectable self-assembling peptide nanofibers create intramyocardial microenvironments for endothelial cells. Circulation 111(4), 442-450 (2005).
    • (2005) Circulation , vol.111 , Issue.4 , pp. 442-450
    • Davis, M.E.1    Motion, J.P.2    Narmoneva, D.A.3
  • 34
    • 54949097679 scopus 로고    scopus 로고
    • Designer self-assembling peptide nanofiber scaffolds for adult mouse neural stem cell 3-dimensional cultures
    • Gelain F, Bottai D, Vescovi A, Zhang S. Designer self-assembling peptide nanofiber scaffolds for adult mouse neural stem cell 3-dimensional cultures. PLoS ONE 1(1), e119 (2006).
    • (2006) PLoS ONE , vol.1 , Issue.1
    • Gelain, F.1    Bottai, D.2    Vescovi, A.3    Zhang, S.4
  • 35
    • 80155147119 scopus 로고    scopus 로고
    • 3D culture of adult mouse neural stem cells within functionalized self-assembling peptide scaffolds
    • Cunha C, Panseri S, Villa O, Silva D, Gelain F. 3D culture of adult mouse neural stem cells within functionalized self-assembling peptide scaffolds. Int. J. Nanomedicine 6, 943-955 (2011).
    • (2011) Int. J. Nanomedicine , vol.6 , pp. 943-955
    • Cunha, C.1    Panseri, S.2    Villa, O.3    Silva, D.4    Gelain, F.5
  • 36
    • 36749028224 scopus 로고    scopus 로고
    • Reknitting the injured spinal cord by self-assembling peptide nanofiber scaffold
    • Guo J, Su H, Zeng Y et al. Reknitting the injured spinal cord by self-assembling peptide nanofiber scaffold. Nanomedicine 3(4), 311-321 (2007).
    • (2007) Nanomedicine , vol.3 , Issue.4 , pp. 311-321
    • Guo, J.1    Su, H.2    Zeng, Y.3
  • 37
    • 33845287137 scopus 로고    scopus 로고
    • Nano hemostat solution: Immediate hemostasis at the nanoscale
    • Ellis-Behnke RG, Liang YX, Tay DKC et al. Nano hemostat solution: immediate hemostasis at the nanoscale. Nanomedicine 2(4), 207-215 (2006).
    • (2006) Nanomedicine , vol.2 , Issue.4 , pp. 207-215
    • Ellis-Behnke, R.G.1    Liang, Y.X.2    Dkc, T.3
  • 38
    • 75749124231 scopus 로고    scopus 로고
    • Hemostatic efficacy of biological self-assembling peptide nanofibers in a rat kidney model
    • Song H, Zhang L, Zhao X. Hemostatic efficacy of biological self-assembling peptide nanofibers in a rat kidney model. Macromol. Biosci. 10(1), 33-39 (2010).
    • (2010) Macromol. Biosci , vol.10 , Issue.1 , pp. 33-39
    • Song, H.1    Zhang, L.2    Zhao, X.3
  • 39
    • 10644264493 scopus 로고    scopus 로고
    • The effect of functionalized self-assembling peptide scaffolds on human aortic endothelial cell function
    • Genové E, Shen C, Zhang S, Semino CE. The effect of functionalized self-assembling peptide scaffolds on human aortic endothelial cell function. Biomaterials 26(16), 3341-3351 (2005).
    • (2005) Biomaterials , vol.26 , Issue.16 , pp. 3341-3351
    • Genové, E.1    Shen, C.2    Zhang, S.3    Semino, C.E.4
  • 40
    • 52449088062 scopus 로고    scopus 로고
    • Self-assembling peptide nanofibers and skeletal myoblast transplantation in infarcted myocardium
    • Dubois G, Segers VFM, Bellamy V et al. Self-assembling peptide nanofibers and skeletal myoblast transplantation in infarcted myocardium. J. Biomed. Mater. Res. Part B Appl. Biomater. 87(1), 222-228 (2008
    • (2008) J. Biomed. Mater. Res. Part B Appl. Biomater , vol.87 , Issue.1 , pp. 222-228
    • Dubois, G.1    Vfm, S.2    Bellamy, V.3
  • 41
    • 65949099307 scopus 로고    scopus 로고
    • The effect of a self-assembling peptide nanofiber scaffold (peptide) when used as a wound dressing for the treatment of deep second degree burns in rats
    • Meng H, Chen L, Ye Z, Wang S, Zhao X. The effect of a self-assembling peptide nanofiber scaffold (peptide) when used as a wound dressing for the treatment of deep second degree burns in rats. J. Biomed. Mater. Res. Part B Appl. Biomater. 89(2), 379-391 (2008).
    • (2008) J. Biomed. Mater. Res. Part B Appl. Biomater , vol.89 , Issue.2 , pp. 379-391
    • Meng, H.1    Chen, L.2    Ye, Z.3    Wang, S.4    Zhao, X.5
  • 42
    • 70350504456 scopus 로고    scopus 로고
    • Construction of synthetic dermis and skin based on a self-assembled peptide hydrogel scaffold
    • Kao B, Kadomatsu K, Hosaka Y. Construction of synthetic dermis and skin based on a self-assembled peptide hydrogel scaffold. Tissue Eng. Part A 15(9), 2385-2396 (2009).
    • (2009) Tissue Eng. Part A , vol.15 , Issue.9 , pp. 2385-2396
    • Kao, B.1    Kadomatsu, K.2    Hosaka, Y.3
  • 43
    • 33746846132 scopus 로고    scopus 로고
    • Self-assembling b-sheet tape forming peptides
    • Davies RPW, Aggeli A, Beevers AJ et al. Self-assembling b-sheet tape forming peptides. Supramol. Chem. 18(5), 435-443 (2006).
    • (2006) Supramol. Chem , vol.18 , Issue.5 , pp. 435-443
    • Rpw, D.1    Aggeli, A.2    Beevers, A.J.3
  • 44
    • 0035834113 scopus 로고    scopus 로고
    • Hierarchical self-assembly of chiral rod-like molecules as a model for peptide b-sheet tapes, ribbons, fibrils, and fibers
    • Aggeli A, Nyrkova IA, Bell M et al. Hierarchical self-assembly of chiral rod-like molecules as a model for peptide b-sheet tapes, ribbons, fibrils, and fibers. Proc. Natl Acad. Sci. USA 98(21), 11857-11862 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , Issue.21 , pp. 11857-11862
    • Aggeli, A.1    Nyrkova, I.A.2    Bell, M.3
  • 45
    • 0043127093 scopus 로고    scopus 로고
    • PH as a trigger of peptide b-sheet self-assembly and reversible switching between nematic and isotropic phases
    • Aggeli A, Bell M, Carrick LM et al. pH as a trigger of peptide b-sheet self-assembly and reversible switching between nematic and isotropic phases. J. Am. Chem. Soc. 125(32), 9619-9628 (2003).
    • (2003) J. Am. Chem. Soc , vol.125 , Issue.32 , pp. 9619-9628
    • Aggeli, A.1    Bell, M.2    Carrick, L.M.3
  • 46
    • 34250660127 scopus 로고    scopus 로고
    • Effect of ionic strength on the self-assembly, morphology and gelation of pH responsive b-sheet tape-forming peptides
    • Carrick LM, Aggeli A, Boden N et al. Effect of ionic strength on the self-assembly, morphology and gelation of pH responsive b-sheet tape-forming peptides. Tetrahedron 63(31), 7457-7467 (2007).
    • (2007) Tetrahedron , vol.63 , Issue.31 , pp. 7457-7467
    • Carrick, L.M.1    Aggeli, A.2    Boden, N.3
  • 47
    • 0345530074 scopus 로고    scopus 로고
    • Self-assembling peptide polyelectrolyte b-sheet complexes form nematic hydrogels
    • Aggeli A, Bell M, Boden N, Carrick LM, Strong AE. Self-assembling peptide polyelectrolyte b-sheet complexes form nematic hydrogels. Angew. Chem. Int. Ed. 42(45), 5603-5606 (2003).
    • (2003) Angew. Chem. Int. Ed , vol.42 , Issue.45 , pp. 5603-5606
    • Aggeli, A.1    Bell, M.2    Boden, N.3    Carrick, L.M.4    Strong, A.E.5
  • 48
    • 85015494235 scopus 로고    scopus 로고
    • The biocompatibility and immunogenicity of self-assembling peptides for use in tissue engineering and regenerative applications
    • Wilshaw SP, Aggeli A, Fisher J, Ingham E. The biocompatibility and immunogenicity of self-assembling peptides for use in tissue engineering and regenerative applications. Tissue Eng. Part A 14(5), 785-785 (2008).
    • (2008) Tissue Eng. Part A , vol.14 , Issue.5 , pp. 785-785
    • Wilshaw, S.P.1    Aggeli, A.2    Fisher, J.3    Ingham, E.4
  • 49
    • 80052538423 scopus 로고    scopus 로고
    • De novo designed positively charged tape-forming peptides: Self-assembly and gelation in physiological solutions and their evaluation as matrices for cell growth
    • Maude S, Miles DE, Felton SH et al. De novo designed positively charged tape-forming peptides: self-assembly and gelation in physiological solutions and their evaluation as matrices for cell growth. Soft Matter 7, 8085-8099 (2011).
    • (2011) Soft Matter , vol.7 , pp. 8085-8099
    • Maude, S.1    De, M.2    Felton, S.H.3
  • 50
    • 77049125455 scopus 로고    scopus 로고
    • Interaction of self-assembling b-sheet peptides with phospholipid monolayers: The effect of serine, threonine, glutamine and asparagine amino acid side chains
    • Protopapa E, Ringstad L, Aggeli A, Nelson A. Interaction of self-assembling b-sheet peptides with phospholipid monolayers: the effect of serine, threonine, glutamine and asparagine amino acid side chains. Electrochim. Acta 55(9), 3368-3375 (2010).
    • (2010) Electrochim. Acta , vol.55 , Issue.9 , pp. 3368-3375
    • Protopapa, E.1    Ringstad, L.2    Aggeli, A.3    Nelson, A.4
  • 51
    • 0037778904 scopus 로고    scopus 로고
    • Enzymatic modification of self-assembled peptide structures with tissue transglutaminase
    • Collier JH, Messersmith PB. Enzymatic modification of self-assembled peptide structures with tissue transglutaminase. Bioconjugate Chem. 14(4), 748-755 (2003).
    • (2003) Bioconjugate Chem , vol.14 , Issue.4 , pp. 748-755
    • Collier, J.H.1    Messersmith, P.B.2
  • 52
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson PE, Muir TW, Clark-Lewis I, Kent SBH. Synthesis of proteins by native chemical ligation. Science 266(5186), 776-779 (1994).
    • (1994) Science , vol.266 , Issue.5186 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.H.4
  • 53
    • 40049102344 scopus 로고    scopus 로고
    • Modulating the mechanical properties of self-assembled peptide hydrogels via native chemical ligation
    • Jung JP, Jones JL, Cronier SA, Collier JH. Modulating the mechanical properties of self-assembled peptide hydrogels via native chemical ligation. Biomaterials 29(13), 2143-2151 (2008).
    • (2008) Biomaterials , vol.29 , Issue.13 , pp. 2143-2151
    • Jung, J.P.1    Jones, J.L.2    Cronier, S.A.3    Collier, J.H.4
  • 54
    • 60549106355 scopus 로고    scopus 로고
    • Co-assembling peptides as defined matrices for endothelial cells
    • Jung JP, Nagaraj AK, Fox EK et al. Co-assembling peptides as defined matrices for endothelial cells. Biomaterials 30(12), 2400-2410 (2009).
    • (2009) Biomaterials , vol.30 , Issue.12 , pp. 2400-2410
    • Jung, J.P.1    Nagaraj, A.K.2    Fox, E.K.3
  • 55
    • 18644373288 scopus 로고    scopus 로고
    • Ile-Lys- Val-Ala-Val (IKVAV)-containing laminin a1 chain peptides form amyloid-like fibrils
    • Yamada M, Kadoya Y, Kasai S et al. Ile-Lys- Val-Ala-Val (IKVAV)-containing laminin a1 chain peptides form amyloid-like fibrils. FEBS Lett. 530(1-3), 48-52 (2002).
    • (2002) FEBS Lett , vol.530 , Issue.1-3 , pp. 48-52
    • Yamada, M.1    Kadoya, Y.2    Kasai, S.3
  • 56
    • 1542740080 scopus 로고    scopus 로고
    • Multifunctional peptide fibrils for biomedical materials
    • Kasai S, Ohga Y, Mochizuki M et al. Multifunctional peptide fibrils for biomedical materials. Peptide Sci. 76(1), 27-33 (2004).
    • (2004) Peptide Sci , vol.76 , Issue.1 , pp. 27-33
    • Kasai, S.1    Ohga, Y.2    Mochizuki, M.3
  • 57
    • 70349881784 scopus 로고    scopus 로고
    • Design and activity of multifunctional fibrils using receptor-specific small peptides
    • Ohga Y, Katagiri F, Takeyama K et al. Design and activity of multifunctional fibrils using receptor-specific small peptides. Biomaterials 30(35), 6731-6738 (2009).
    • (2009) Biomaterials , vol.30 , Issue.35 , pp. 6731-6738
    • Ohga, Y.1    Katagiri, F.2    Takeyama, K.3
  • 58
    • 38749119393 scopus 로고    scopus 로고
    • Functionalised amyloid fibrils for roles in cell adhesion
    • Gras SL, Tickler AK, Squires AM et al. Functionalised amyloid fibrils for roles in cell adhesion. Biomaterials 29(11), 1553-1562 (2008).
    • (2008) Biomaterials , vol.29 , Issue.11 , pp. 1553-1562
    • Gras, S.L.1    Tickler, A.K.2    Squires, A.M.3
  • 59
    • 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 et al. Arg-Gly-Asp constrained within cyclic pentapeptides: strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1. FEBS Lett. 291(1), 50-54 (1991).
    • (1991) FEBS Lett , vol.291 , Issue.1 , pp. 50-54
    • Aumailley, M.1    Gurrath, M.2    Muller, G.3
  • 60
    • 79959875103 scopus 로고    scopus 로고
    • Functional fibrils derived from the peptide TTR1-cycloRGDfK that target cell adhesion and spreading
    • Bongiovanni MN, Scanlon DB, Gras SL. Functional fibrils derived from the peptide TTR1-cycloRGDfK that target cell adhesion and spreading. Biomaterials 32(26), 6099-6110 (2011).
    • (2011) Biomaterials , vol.32 , Issue.26 , pp. 6099-6110
    • Bongiovanni, M.N.1    Scanlon, D.B.2    Gras, S.L.3
  • 61
    • 79952937011 scopus 로고    scopus 로고
    • BMHP1-derived self-assembling peptides: Hierarchically assembled structures with self-healing propensity and potential for tissue engineering applications
    • Gelain F, Silva D, Caprini A et al. BMHP1-derived self-assembling peptides: hierarchically assembled structures with self-healing propensity and potential for tissue engineering applications. ACS Nano 5(3), 1845-1859 (2011).
    • (2011) ACS Nano , vol.5 , Issue.3 , pp. 1845-1859
    • Gelain, F.1    Silva, D.2    Caprini, A.3
  • 62
    • 67649998195 scopus 로고    scopus 로고
    • Effect of functionalization on the self-assembling propensity of b-sheet forming peptides
    • Taraballi F, Campione M, Sassella A et al. Effect of functionalization on the self-assembling propensity of b-sheet forming peptides. Soft Matter 5(3), 660-668 (2009).
    • (2009) Soft Matter , vol.5 , Issue.3 , pp. 660-668
    • Taraballi, F.1    Campione, M.2    Sassella, A.3
  • 63
    • 0037132592 scopus 로고    scopus 로고
    • Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide
    • Schneider JP, Pochan DJ, Ozbas B et al. Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide. J. Am. Chem. Soc. 124(50), 15030-15037 (2002).
    • (2002) J. Am. Chem. Soc , vol.124 , Issue.50 , pp. 15030-15037
    • Schneider, J.P.1    Pochan, D.J.2    Ozbas, B.3
  • 64
    • 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 37(19), 7331-7337 (2004).
    • (2004) Macromolecules , vol.37 , Issue.19 , pp. 7331-7337
    • Ozbas, B.1    Kretsinger, J.2    Rajagopal, K.3    Schneider, J.P.4    Pochan, D.J.5
  • 65
    • 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 et al. Controlling hydrogelation kinetics by peptide design for three-dimensional encapsulation and injectable delivery of cells. Proc. Natl Acad. Sci. USA 104(19), 7791-7796 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.19 , pp. 7791-7796
    • Haines-Butterick, L.1    Rajagopal, K.2    Branco, M.3
  • 66
  • 67
    • 36749074939 scopus 로고    scopus 로고
    • Inherent antibacterial activity of a peptide-based b-hairpin hydrogel
    • Salick DA, Kretsinger JK, Pochan DJ, Schneider JP. Inherent antibacterial activity of a peptide-based b-hairpin hydrogel. J. Am. Chem. Soc. 129(47), 14793-14799 (2007).
    • (2007) J. Am. Chem. Soc , vol.129 , Issue.47 , pp. 14793-14799
    • Salick, D.A.1    Kretsinger, J.K.2    Pochan, D.J.3    Schneider, J.P.4
  • 68
    • 49349105563 scopus 로고    scopus 로고
    • In vitro assessment of the pro-inflammatory potential of b-hairpin peptide hydrogels
    • Haines-Butterick LA, Salick DA, Pochan DJ, Schneider JP. In vitro assessment of the pro-inflammatory potential of b-hairpin peptide hydrogels. Biomaterials 29(31), 4164-4169 (2008).
    • (2008) Biomaterials , vol.29 , Issue.31 , pp. 4164-4169
    • Haines-Butterick, L.A.1    Salick, D.A.2    Pochan, D.J.3    Schneider, J.P.4
  • 69
    • 0025272940 scopus 로고
    • A-helical coiled coils and bundles: How to design an a-helical protein
    • Cohen C, Parry DAD. a-helical coiled coils and bundles: how to design an a-helical protein. Proteins Struct. Funct. Genet. 7(1), 1-15 (1990).
    • (1990) Proteins Struct. Funct. Genet , vol.7 , Issue.1 , pp. 1-15
    • Cohen, C.1    Dad, P.2
  • 70
    • 67649550660 scopus 로고    scopus 로고
    • Rational design and application of responsive a-helical peptide hydrogels
    • Banwell EF, Abelardo ES, Adams DJ et al. Rational design and application of responsive a-helical peptide hydrogels. Nat. Mater. 8(7), 596-600 (2009).
    • (2009) Nat. Mater , vol.8 , Issue.7 , pp. 596-600
    • Banwell, E.F.1    Abelardo, E.S.2    Adams, D.J.3
  • 71
    • 1442359484 scopus 로고    scopus 로고
    • Shift of fibril-forming ability of the designed a-helical coiled-coil peptides into the physiological pH region
    • Melnik TN, Villard V, Vasiliev V et al. Shift of fibril-forming ability of the designed a-helical coiled-coil peptides into the physiological pH region. Protein Eng. 16(12), 1125-1130 (2003).
    • (2003) Protein Eng , vol.16 , Issue.12 , pp. 1125-1130
    • Melnik, T.N.1    Villard, V.2    Vasiliev, V.3
  • 72
    • 33644790664 scopus 로고    scopus 로고
    • Synthetic RGD-containing a-helical coiled coil peptides promote integrin-dependent cell adhesion
    • Villard V, Kalyuzhniy O, Riccio O et al. Synthetic RGD-containing a-helical coiled coil peptides promote integrin-dependent cell adhesion. J. Pept. Sci. 12(3), 206-212 (2006).
    • (2006) J. Pept. Sci , vol.12 , Issue.3 , pp. 206-212
    • Villard, V.1    Kalyuzhniy, O.2    Riccio, O.3
  • 73
    • 23344437452 scopus 로고    scopus 로고
    • Self-assembly of peptide nanotubes and amyloid-like structures by charged-termini-capped diphenylalanine peptide analogues
    • Reches M, Gazit E. Self-assembly of peptide nanotubes and amyloid-like structures by charged-termini-capped diphenylalanine peptide analogues. Isr. J. Chem. 45(3), 363-371 (2005).
    • (2005) Isr. J. Chem , vol.45 , Issue.3 , pp. 363-371
    • Reches, M.1    Gazit, E.2
  • 74
    • 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. 18(11), 1365-1370 (2006).
    • (2006) Adv. Mater , vol.18 , Issue.11 , pp. 1365-1370
    • Mahler, A.1    Reches, M.2    Rechter, M.3    Cohen, S.4    Gazit, E.5
  • 75
    • 0029395701 scopus 로고
    • Use of a gel-forming dipeptide derivative as a carrier for antigen presentation
    • Vegners R, Shestakova I, Kalvinsh I, Ezzell RM, Janmey PA. Use of a gel-forming dipeptide derivative as a carrier for antigen presentation. J. Pept. Sci. 1(6), 371-378 (1995).
    • (1995) J. Pept. Sci , vol.1 , Issue.6 , pp. 371-378
    • Vegners, R.1    Shestakova, I.2    Kalvinsh, I.3    Ezzell, R.M.4    Janmey, P.A.5
  • 76
    • 0242490652 scopus 로고    scopus 로고
    • Supramolecular hydrogels respond to ligand- receptor interaction
    • Zhang Y, Gu H, Yang Z, Xu B. Supramolecular hydrogels respond to ligand- receptor interaction. J. Am. Chem. Soc. 125(45), 13680-13681 (2003).
    • (2003) J. Am. Chem. Soc , vol.125 , Issue.45 , pp. 13680-13681
    • Zhang, Y.1    Gu, H.2    Yang, Z.3    Xu, B.4
  • 77
    • 33644913129 scopus 로고    scopus 로고
    • Nanostructured hydrogels for three-dimensional cell culture through self-assembly of fluorenylmethoxycarbonyl-dipeptides
    • Jayawarna V, Ali M, Jowitt TA et al. Nanostructured hydrogels for three-dimensional cell culture through self-assembly of fluorenylmethoxycarbonyl-dipeptides. Adv. Mater. 18(5), 611-614 (2006).
    • (2006) Adv. Mater , vol.18 , Issue.5 , pp. 611-614
    • Jayawarna, V.1    Ali, M.2    Jowitt, T.A.3
  • 78
    • 60849093458 scopus 로고    scopus 로고
    • Self-assembled peptide-based hydrogels as scaffolds for anchorage-dependent cells
    • Zhou M, Smith AM, Das AK et al. Self-assembled peptide-based hydrogels as scaffolds for anchorage-dependent cells. Biomaterials 30(13), 2523-2530 (2009).
    • (2009) Biomaterials , vol.30 , Issue.13 , pp. 2523-2530
    • Zhou, M.1    Smith, A.M.2    Das, A.K.3
  • 79
    • 34248198964 scopus 로고    scopus 로고
    • Enzymatic control of the self-assembly of small molecules: A new way to generate supramolecular hydrogels
    • Yang ZM, Liang GL, Xu B. Enzymatic control of the self-assembly of small molecules: a new way to generate supramolecular hydrogels. Soft Matter 3(5), 515-520 (2007).
    • (2007) Soft Matter , vol.3 , Issue.5 , pp. 515-520
    • Yang, Z.M.1    Liang, G.L.2    Xu, B.3
  • 80
    • 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. 128(4), 1070-1071 (2006).
    • (2006) J. Am. Chem. Soc , vol.128 , Issue.4 , pp. 1070-1071
    • Toledano, S.1    Williams, R.J.2    Jayawarna, V.3    Ulijn, R.V.4
  • 81
    • 38449096286 scopus 로고    scopus 로고
    • Fmoc-diphenylalanine self assembles to a hydrogel via a novel architecture based on p-p interlocked b-sheets
    • Smith AM, Williams RJ, Tang C et al. Fmoc-diphenylalanine self assembles to a hydrogel via a novel architecture based on p-p interlocked b-sheets. Adv. Mater. 20(1), 37-41 (2008).
    • (2008) Adv. Mater , vol.20 , Issue.1 , pp. 37-41
    • Smith, A.M.1    Williams, R.J.2    Tang, C.3
  • 82
    • 84869030248 scopus 로고    scopus 로고
    • Experimental and computational studies reveal an alternative supramolecular structure for Fmoc-dipeptide self-assembly
    • Mu XJ, Eckes KM, Nguyen MM, Suggs LJ, Ren PY. Experimental and computational studies reveal an alternative supramolecular structure for Fmoc-dipeptide self-assembly. Biomacromolecules 13(11), 3562-3571 (2012).
    • (2012) Biomacromolecules , vol.13 , Issue.11 , pp. 3562-3571
    • Mu, X.J.1    Eckes, K.M.2    Nguyen, M.M.3    Suggs, L.J.4    Ren, P.Y.5
  • 83
    • 39049149107 scopus 로고    scopus 로고
    • Self-assembling Fmoc dipeptide hydrogel for in situ 3D cell culturing
    • Liebmann T, Rydholm S, Akpe V, Brismar H. Self-assembling Fmoc dipeptide hydrogel for in situ 3D cell culturing. BMC Biotechnol. 7, 88 (2007).
    • (2007) BMC Biotechnol , vol.7 , pp. 88
    • Liebmann, T.1    Rydholm, S.2    Akpe, V.3    Brismar, H.4
  • 84
    • 60649121345 scopus 로고    scopus 로고
    • Introducing chemical functionality in Fmoc-peptide gels for cell culture
    • Jayawarna V, Richardson SM, Hirst AR et al. Introducing chemical functionality in Fmoc-peptide gels for cell culture. Acta Biomater. 5(3), 934-943 (2009).
    • (2009) Acta Biomater , vol.5 , Issue.3 , pp. 934-943
    • Jayawarna, V.1    Richardson, S.M.2    Hirst, A.R.3
  • 85
    • 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 126(4), 677-689 (2006).
    • (2006) Cell , vol.126 , Issue.4 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 86
    • 84855446857 scopus 로고    scopus 로고
    • Fmoc-diphenylalanine hydrogels: Understanding the variability in reported mechanical properties
    • Raeburn J, Pont G, Chen L et al. Fmoc-diphenylalanine hydrogels: understanding the variability in reported mechanical properties. Soft Matter 8(4), 1168-1174 (2012).
    • (2012) Soft Matter , vol.8 , Issue.4 , pp. 1168-1174
    • Raeburn, J.1    Pont, G.2    Chen, L.3
  • 87
    • 79951906149 scopus 로고    scopus 로고
    • Mechanosensitive peptide gelation: Mode of agitation controls mechanical properties and nano-scale morphology
    • Helen W, de Leonardis P, Ulijn RV, Gough J, Tirelli N. Mechanosensitive peptide gelation: mode of agitation controls mechanical properties and nano-scale morphology. Soft Matter 7, 1732-1740 (2011).
    • (2011) Soft Matter , vol.7 , pp. 1732-1740
    • Helen, W.1    De Leonardis, P.2    Ulijn, R.V.3    Gough, J.4    Tirelli, N.5
  • 88
    • 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 et al. A new method for maintaining homogeneity during liquid-hydrogel transitions using low molecular weight hydrogelators. Soft Matter 5(9), 1856-1862 (2009).
    • (2009) Soft Matter , vol.5 , Issue.9 , pp. 1856-1862
    • Adams, D.J.1    Butler, M.F.2    Frith, W.J.3
  • 89
    • 33845954636 scopus 로고    scopus 로고
    • The role of hydrophobicity in toxicity prediction
    • Cronin MTD. The role of hydrophobicity in toxicity prediction. Curr. Comput. Aided Drug Des. 2(4), 405-413 (2006).
    • (2006) Curr. Comput. Aided Drug des , vol.2 , Issue.4 , pp. 405-413
    • Mtd, C.1
  • 90
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley WC, White SH. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3(10), 842-848 (1996).
    • (1996) Nat. Struct. Biol , vol.3 , Issue.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 91
    • 70349191453 scopus 로고    scopus 로고
    • Self-assembled Fmoc-peptides as a platform for the formation of nanostructures and hydrogels
    • Orbach R, Adler-Abramovich L, Zigerson S et al. Self-assembled Fmoc-peptides as a platform for the formation of nanostructures and hydrogels. Biomacromolecules 10(9), 2646-2651 (2009).
    • (2009) Biomacromolecules , vol.10 , Issue.9 , pp. 2646-2651
    • Orbach, R.1    Adler-Abramovich, L.2    Zigerson, S.3
  • 93
    • 84856481596 scopus 로고    scopus 로고
    • The rheological and structural properties of Fmoc-peptide-based hydrogels: The effect of aromatic molecular architecture on self-assembly and physical characteristics
    • Orbach R, Mironi-Harpaz I, Adler-Abramovich L et al. The rheological and structural properties of Fmoc-peptide-based hydrogels: the effect of aromatic molecular architecture on self-assembly and physical characteristics. Langmuir 28(4), 2015-2022 (2012).
    • (2012) Langmuir , vol.28 , Issue.4 , pp. 2015-2022
    • Orbach, R.1    Mironi-Harpaz, I.2    Adler-Abramovich, L.3
  • 94
    • 82355175365 scopus 로고    scopus 로고
    • Self-assembly of Fmoc-tetrapeptides based on the RGDS cell adhesion motif
    • Castelletto V, Moulton CM, Cheng G et al. Self-assembly of Fmoc-tetrapeptides based on the RGDS cell adhesion motif. Soft Matter 7(24), 11405-11415 (2011).
    • (2011) Soft Matter , vol.7 , Issue.24 , pp. 11405-11415
    • Castelletto, V.1    Moulton, C.M.2    Cheng, G.3
  • 96
    • 0038789021 scopus 로고    scopus 로고
    • Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction
    • Niece KL, Hartgerink JD, Donners JJJM, Stupp SI. Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction. J. Am. Chem. Soc. 125(24), 7146-7147 (2003).
    • (2003) J. Am. Chem. Soc , vol.125 , Issue.24 , pp. 7146-7147
    • Niece, K.L.1    Hartgerink, J.D.2    Jjjm, D.3    Stupp, S.I.4
  • 97
    • 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 294(5547), 1684-1688 (2001).
    • (2001) Science , vol.294 , Issue.5547 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 98
    • 1442281238 scopus 로고    scopus 로고
    • Selective differentiation of neural progenitor cells by high-epitope density nanofibers
    • Silva GA, Czeisler C, Niece KL et al. Selective differentiation of neural progenitor cells by high-epitope density nanofibers. Science 303(5662), 1352-1355 (2004).
    • (2004) Science , vol.303 , Issue.5662 , pp. 1352-1355
    • Silva, G.A.1    Czeisler, C.2    Niece, K.L.3
  • 99
    • 43649108455 scopus 로고    scopus 로고
    • Self-assembling nanofibers inhibit glial scar formation and promote axon elongation after spinal cord injury
    • Tysseling-Mattiace VM, Sahni V, Niece KL et al. Self-assembling nanofibers inhibit glial scar formation and promote axon elongation after spinal cord injury. J. Neurosci. 28(14), 3814-3823 (2008).
    • (2008) J. Neurosci , vol.28 , Issue.14 , pp. 3814-3823
    • Tysseling-Mattiace, V.M.1    Sahni, V.2    Niece, K.L.3
  • 100
    • 34547916493 scopus 로고    scopus 로고
    • Supramolecular crafting of cell adhesion
    • Storrie H, Guler MO, Abu-Amara SN et al. Supramolecular crafting of cell adhesion. Biomaterials 28(31), 4608-4618 (2007).
    • (2007) Biomaterials , vol.28 , Issue.31 , pp. 4608-4618
    • Storrie, H.1    Guler, M.O.2    Abu-Amara, S.N.3
  • 101
    • 77953909551 scopus 로고    scopus 로고
    • A self-assembly pathway to aligned monodomain gels
    • Zhang S, Greenfield MA, Mata A et al. A self-assembly pathway to aligned monodomain gels. Nat. Mater. 9, 594-601 (2010).
    • (2010) Nat. Mater , vol.9 , pp. 594-601
    • Zhang, S.1    Greenfield, M.A.2    Mata, A.3
  • 102
    • 62249111329 scopus 로고    scopus 로고
    • Micropatterning of bioactive self-assembling gels
    • Mata A, Hsu L, Capito R et al. Micropatterning of bioactive self-assembling gels. Soft Matter 5(6), 1228-1236 (2009).
    • (2009) Soft Matter , vol.5 , Issue.6 , pp. 1228-1236
    • Mata, A.1    Hsu, L.2    Capito, R.3
  • 103
  • 104
    • 0032715155 scopus 로고    scopus 로고
    • Trifluoroacetate, a contaminant in purified proteins, inhibits proliferation of osteoblasts and chondrocytes
    • Cornish J, Callon KE, Lin CQX et al. Trifluoroacetate, a contaminant in purified proteins, inhibits proliferation of osteoblasts and chondrocytes. Am. J. Physiol. Endocrinol. Metabol. 277(5), E779-E783 (1999).
    • (1999) Am. J. Physiol. Endocrinol. Metabol , vol.277 , Issue.5
    • Cornish, J.1    Callon, K.E.2    Cqx, L.3
  • 105
    • 33846680089 scopus 로고    scopus 로고
    • Optimization of the hydrochloric acid concentration used for trifluoroacetate removal from synthetic peptides
    • Andrushchenko VV, Vogel HJ, Prenner EJ. Optimization of the hydrochloric acid concentration used for trifluoroacetate removal from synthetic peptides. J. Pept. Sci. 13(1), 37-43 (2007).
    • (2007) J. Pept. Sci , vol.13 , Issue.1 , pp. 37-43
    • Andrushchenko, V.V.1    Vogel, H.J.2    Prenner, E.J.3
  • 106
    • 40749109792 scopus 로고    scopus 로고
    • Elimination and exchange of trifluoroacetate counter-ion from cationic peptides: A critical evaluation of different approaches
    • Roux S, Zékri E, Rousseau B et al. Elimination and exchange of trifluoroacetate counter-ion from cationic peptides: a critical evaluation of different approaches. J. Pept. Sci. 14(3), 354-359 (2008).
    • (2008) J. Pept. Sci , vol.14 , Issue.3 , pp. 354-359
    • Roux, S.1    Zékri, E.2    Rousseau, B.3
  • 107
    • 68649108646 scopus 로고    scopus 로고
    • Fmoc-diphenylalanine self-assembly mechanism induces apparent pKa shifts
    • Tang C, Smith AM, Collins RF, Ulijn RV, Saiani A. Fmoc-diphenylalanine self-assembly mechanism induces apparent pKa shifts. Langmuir 25(16), 9447-9453 (2009).
    • (2009) Langmuir , vol.25 , Issue.16 , pp. 9447-9453
    • Tang, C.1    Smith, A.M.2    Collins, R.F.3    Ulijn, R.V.4    Saiani, A.5
  • 108
    • 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 310(5751), 1139-1143 (2005).
    • (2005) Science , vol.310 , Issue.5751 , pp. 1139-1143
    • De, D.1    Janmey, P.2    Wang, Y.L.3
  • 109
    • 77951228475 scopus 로고    scopus 로고
    • Mechanical control of tissue and organ development
    • Mammoto T, Ingber DE. Mechanical control of tissue and organ development. Development 137(9), 1407-1420 (2010).
    • (2010) Development , vol.137 , Issue.9 , pp. 1407-1420
    • Mammoto, T.1    Ingber, D.E.2
  • 110
    • 0041559949 scopus 로고    scopus 로고
    • RGD modified polymers: Biomaterials for stimulated cell adhesion and beyond
    • Hersel U, Dahmen C, Kessler H. RGD modified polymers: biomaterials for stimulated cell adhesion and beyond. Biomaterials 24(24), 4385-4415 (2003).
    • (2003) Biomaterials , vol.24 , Issue.24 , pp. 4385-4415
    • Hersel, U.1    Dahmen, C.2    Kessler, H.3
  • 111
    • 0026468460 scopus 로고
    • Functional domains of cell adhesion molecules
    • Yamada Y, Kleinman HK. Functional domains of cell adhesion molecules. Curr. Opin. Cell Biol. 4(5), 819-823 (1992).
    • (1992) Curr. Opin. Cell Biol , vol.4 , Issue.5 , pp. 819-823
    • Yamada, Y.1    Kleinman, H.K.2
  • 112
    • 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. 12, 697-715 (1996).
    • (1996) Annu. Rev. Cell Dev. Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 113
    • 79955095820 scopus 로고    scopus 로고
    • The role of short synthetic adhesion peptides in regenerative medicine; The debate
    • Williams DF. The role of short synthetic adhesion peptides in regenerative medicine; the debate. Biomaterials 32(18), 4195-4197 (2011).
    • (2011) Biomaterials , vol.32 , Issue.18 , pp. 4195-4197
    • Williams, D.F.1
  • 114
    • 79955095294 scopus 로고    scopus 로고
    • Evolving the use of peptides as components of biomaterials
    • Collier JH, Segura T. Evolving the use of peptides as components of biomaterials. Biomaterials 32(18), 4198-4204 (2011).
    • (2011) Biomaterials , vol.32 , Issue.18 , pp. 4198-4204
    • Collier, J.H.1    Segura, T.2
  • 115
    • 0036901990 scopus 로고    scopus 로고
    • Amyloid architecture: Complementary assembly of heterogeneous combinations of three or four peptides into amyloid fibrils
    • Takahashi Y, Ueno A, Mihara H. Amyloid architecture: complementary assembly of heterogeneous combinations of three or four peptides into amyloid fibrils. ChemBioChem 3(7), 637-642 (2002).
    • (2002) ChemBioChem , vol.3 , Issue.7 , pp. 637-642
    • Takahashi, Y.1    Ueno, A.2    Mihara, H.3
  • 116
    • 79952517440 scopus 로고    scopus 로고
    • Multifactorial optimization of endothelial cell growth using modular synthetic extracellular matrices
    • Jung JP, Moyano JV, Collier JH. Multifactorial optimization of endothelial cell growth using modular synthetic extracellular matrices. Integr. Biol. 3, 185-196 (2011).
    • (2011) Integr. Biol , vol.3 , pp. 185-196
    • Jung, J.P.1    Moyano, J.V.2    Collier, J.H.3
  • 117
    • 79960080932 scopus 로고    scopus 로고
    • Controlled biodegradation of self-assembling b-hairpin peptide hydrogels by proteolysis with matrix metalloproteinase-13
    • Giano MC, Pochan DJ, Schneider JP. Controlled biodegradation of self-assembling b-hairpin peptide hydrogels by proteolysis with matrix metalloproteinase-13. Biomaterials 32(27), 6471-6477 (2011).
    • (2011) Biomaterials , vol.32 , Issue.27 , pp. 6471-6477
    • Giano, M.C.1    Pochan, D.J.2    Schneider, J.P.3
  • 118
    • 79955120631 scopus 로고    scopus 로고
    • The role of ECM proteins and protein fragments in guiding cell behavior in regenerative medicine
    • Barker TH. The role of ECM proteins and protein fragments in guiding cell behavior in regenerative medicine. Biomaterials 32(18), 4211-4214 (2011).
    • (2011) Biomaterials , vol.32 , Issue.18 , pp. 4211-4214
    • Barker, T.H.1
  • 119
    • 79959525979 scopus 로고    scopus 로고
    • Fibrillized peptide microgels for cell encapsulation and 3D cell culture
    • Tian YF, Devgun JM, Collier JH. Fibrillized peptide microgels for cell encapsulation and 3D cell culture. Soft Matter 7, 6005-6011 (2011).
    • (2011) Soft Matter , vol.7 , pp. 6005-6011
    • Tian, Y.F.1    Devgun, J.M.2    Collier, J.H.3
  • 120
    • 77955279131 scopus 로고    scopus 로고
    • The non-covalent decoration of self-assembling protein fibers
    • Mahmoud ZN, Grundy DJ, Channon KJ, Woolfson DN. The non-covalent decoration of self-assembling protein fibers. Biomaterials 31(29), 7468-7474 (2010).
    • (2010) Biomaterials , vol.31 , Issue.29 , pp. 7468-7474
    • Mahmoud, Z.N.1    Grundy, D.J.2    Channon, K.J.3    Woolfson, D.N.4
  • 121
    • 0000096835 scopus 로고    scopus 로고
    • Click Chemistry: Diverse chemical function from a few good reactions
    • Kolb HC, Finn MG, Sharpless KB. Click Chemistry: diverse chemical function from a few good reactions. Angew. Chem. Int. Ed. 40(11), 2004-2021 (2001).
    • (2001) Angew. Chem. Int. Ed , vol.40 , Issue.11 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 123
    • 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 6(3), 1316-1321 (2005).
    • (2005) Biomacromolecules , vol.6 , Issue.3 , pp. 1316-1321
    • Ramachandran, S.1    Tseng, Y.2    Yu, Y.B.3
  • 124
    • 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. 18(26), 6157-6162 (2006).
    • (2006) Chem. Mater , vol.18 , Issue.26 , pp. 6157-6162
    • Ramachandran, S.1    Trewhella, J.2    Tseng, Y.3    Yu, Y.B.4
  • 125
    • 77954580602 scopus 로고    scopus 로고
    • Effect of temperature during assembly on the structure and mechanical properties of peptide-based materials
    • Ramachandran S, Taraban MB, Trewhella J et al. Effect of temperature during assembly on the structure and mechanical properties of peptide-based materials. Biomacromolecules 11(6), 1502-1506 (2010).
    • (2010) Biomacromolecules , vol.11 , Issue.6 , pp. 1502-1506
    • Ramachandran, S.1    Taraban, M.B.2    Trewhella, J.3
  • 126
    • 84856241045 scopus 로고    scopus 로고
    • Efficacy of self-assembled hydrogels composed of positively or negatively charged peptides as scaffolds for cell culture
    • Nagayasu A, Yokoi H, Minaguchi JA et al. Efficacy of self-assembled hydrogels composed of positively or negatively charged peptides as scaffolds for cell culture. J. Biomater. Appl. 26(6), 651-665 (2012).
    • (2012) J. Biomater. Appl , vol.26 , Issue.6 , pp. 651-665
    • Nagayasu, A.1    Yokoi, H.2    Minaguchi, J.A.3
  • 127
    • 84876730120 scopus 로고    scopus 로고
    • Rational molecular design of complementary self-assembling peptide hydrogels
    • Kyle S, Felton SH, McPherson MJ, Aggeli A, Ingham E. Rational molecular design of complementary self-assembling peptide hydrogels. Adv. Healthcare Mater. 1(5), 640-645 (2012).
    • (2012) Adv. Healthcare Mater , vol.1 , Issue.5 , pp. 640-645
    • Kyle, S.1    Felton, S.H.2    McPherson, M.J.3    Aggeli, A.4    Ingham, E.5
  • 128
    • 84858650309 scopus 로고    scopus 로고
    • Surface-adhesive and osteogenic self-assembled peptide nanofibers for bioinspired functionalization of titanium surfaces
    • Ceylan H, Kocabey S, Tekinay AB, Guler MO. Surface-adhesive and osteogenic self-assembled peptide nanofibers for bioinspired functionalization of titanium surfaces. Soft Matter 8(14), 3929-3937 (2012).
    • (2012) Soft Matter , vol.8 , Issue.14 , pp. 3929-3937
    • Ceylan, H.1    Kocabey, S.2    Tekinay, A.B.3    Guler, M.O.4
  • 129
    • 80053093996 scopus 로고    scopus 로고
    • Selective adhesion and growth of vascular endothelial cells on bioactive peptide nanofiber functionalized stainless steel surface
    • Ceylan H, Tekinay AB, Guler MO. Selective adhesion and growth of vascular endothelial cells on bioactive peptide nanofiber functionalized stainless steel surface. Biomaterials 32(34), 8797-8805 (2011).
    • (2011) Biomaterials , vol.32 , Issue.34 , pp. 8797-8805
    • Ceylan, H.1    Tekinay, A.B.2    Guler, M.O.3
  • 130
    • 37548999304 scopus 로고    scopus 로고
    • Covalent functionalization of NiTi surfaces with bioactive peptide amphiphile nanofibers
    • Sargeant TD, Rao MS, Koh CY, Stupp SI. Covalent functionalization of NiTi surfaces with bioactive peptide amphiphile nanofibers. Biomaterials 29(8), 1085-1098 (2008).
    • (2008) Biomaterials , vol.29 , Issue.8 , pp. 1085-1098
    • Sargeant, T.D.1    Rao, M.S.2    Koh, C.Y.3    Stupp, S.I.4
  • 131
    • 78049417903 scopus 로고    scopus 로고
    • A hybrid biomimetic nanomatrix composed of electrospun polycaprolactone and bioactive peptide amphiphiles for cardiovascular implants
    • Andukuri A, Kushwaha M, Tambralli A et al. A hybrid biomimetic nanomatrix composed of electrospun polycaprolactone and bioactive peptide amphiphiles for cardiovascular implants. Acta Biomater. 7(1), 225-233 (2011).
    • (2011) Acta Biomater , vol.7 , Issue.1 , pp. 225-233
    • Andukuri, A.1    Kushwaha, M.2    Tambralli, A.3
  • 132
    • 33745612238 scopus 로고    scopus 로고
    • Branched peptide-amphiphiles as self-assembling coatings for tissue engineering scaffolds
    • Harrington DA, Cheng EY, Guler MO et al. Branched peptide-amphiphiles as self-assembling coatings for tissue engineering scaffolds. J. Biomed. Mater. Res. Part A 78(1), 157-167 (2006).
    • (2006) J. Biomed. Mater. Res. Part A , vol.78 , Issue.1 , pp. 157-167
    • Harrington, D.A.1    Cheng, E.Y.2    Guler, M.O.3
  • 133
    • 57849116409 scopus 로고    scopus 로고
    • The effect of self-assembling peptide nanofiber scaffolds on mouse embryonic fibroblast implantation and proliferation
    • Dégano IR, Quintana L, Vilalta M et al. The effect of self-assembling peptide nanofiber scaffolds on mouse embryonic fibroblast implantation and proliferation. Biomaterials 30(6), 1156-1165 (2009).
    • (2009) Biomaterials , vol.30 , Issue.6 , pp. 1156-1165
    • Dégano, I.R.1    Quintana, L.2    Vilalta, M.3
  • 135
    • 84857761545 scopus 로고    scopus 로고
    • Modulating adaptive immune responses to peptide self-assemblies
    • Rudra JS, Sun T, Bird KC et al. Modulating adaptive immune responses to peptide self-assemblies. ACS Nano 6(2), 1557-1564 (2012).
    • (2012) ACS Nano , vol.6 , Issue.2 , pp. 1557-1564
    • Rudra, J.S.1    Sun, T.2    Bird, K.C.3
  • 136
    • 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. 16(4), 499-508 (2006).
    • (2006) Adv. Funct. Mater , vol.16 , Issue.4 , pp. 499-508
    • Stendahl, J.C.1    Rao, M.S.2    Guler, M.O.3    Stupp, S.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.