메뉴 건너뛰기




Volumn 102, Issue 7, 2012, Pages 1617-1626

End-to-end self-assembly of RADA 16-I nanofibrils in aqueous solutions

Author keywords

[No Author keywords available]

Indexed keywords

NANOMATERIAL; PEPTIDE; WATER;

EID: 84859406109     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.03.012     Document Type: Article
Times cited : (49)

References (42)
  • 1
    • 33846678796 scopus 로고    scopus 로고
    • Designer self-assembling peptide materials
    • X. Zhao, and S. Zhang Designer self-assembling peptide materials Macromol. Biosci. 7 2007 13 22
    • (2007) Macromol. Biosci. , vol.7 , pp. 13-22
    • Zhao, X.1    Zhang, S.2
  • 2
    • 0036897817 scopus 로고    scopus 로고
    • Design of nanostructured biological materials through self-assembly of peptides and proteins
    • S. Zhang, and D.M. Marini S. Santoso Design of nanostructured biological materials through self-assembly of peptides and proteins Curr. Opin. Chem. Biol. 6 2002 865 871
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 865-871
    • Zhang, S.1    Marini, D.M.2    Santoso, S.3
  • 3
    • 63349111250 scopus 로고    scopus 로고
    • Designer self-assembling peptide nanomaterials
    • Y. Yang, and U. Khoe S. Zhang Designer self-assembling peptide nanomaterials Nano Today 4 2009 193 210
    • (2009) Nano Today , vol.4 , pp. 193-210
    • Yang, Y.1    Khoe, U.2    Zhang, S.3
  • 4
    • 0043127093 scopus 로고    scopus 로고
    • PH as a trigger of peptide β-sheet self-assembly and reversible switching between nematic and isotropic phases
    • A. Aggeli, and M. Bell N. Boden pH as a trigger of peptide β-sheet self-assembly and reversible switching between nematic and isotropic phases J. Am. Chem. Soc. 125 2003 9619 9628
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9619-9628
    • Aggeli, A.1    Bell, M.2    Boden, N.3
  • 5
    • 77955825528 scopus 로고    scopus 로고
    • Molecular self-assembly and applications of designer peptide amphiphiles
    • X. Zhao, and F. Pan J.R. Lu Molecular self-assembly and applications of designer peptide amphiphiles Chem. Soc. Rev. 39 2010 3480 3498
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 3480-3498
    • Zhao, X.1    Pan, F.2    Lu, J.R.3
  • 6
    • 19344363958 scopus 로고    scopus 로고
    • Self-assembly of ionic-complementary peptides: A physicochemical viewpoint
    • P. Chen Self-assembly of ionic-complementary peptides: a physicochemical viewpoint Colloids Surf. A Physicochem. Eng. Asp. 261 2005 3 24
    • (2005) Colloids Surf. A Physicochem. Eng. Asp. , vol.261 , pp. 3-24
    • Chen, P.1
  • 7
    • 77949903483 scopus 로고    scopus 로고
    • Amphiphilic peptides and their cross-disciplinary role as building blocks for nanoscience
    • S. Cavalli, F. Albericio, and A. Kros Amphiphilic peptides and their cross-disciplinary role as building blocks for nanoscience Chem. Soc. Rev. 39 2010 241 263
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 241-263
    • Cavalli, S.1    Albericio, F.2    Kros, A.3
  • 8
    • 63449112991 scopus 로고    scopus 로고
    • Self-assembling properties of ionic-complementary peptides
    • G. D'Auria, and M. Vacatello L. Paolillo Self-assembling properties of ionic-complementary peptides J. Pept. Sci. 15 2009 210 219
    • (2009) J. Pept. Sci. , vol.15 , pp. 210-219
    • D'Auria, G.1    Vacatello, M.2    Paolillo, L.3
  • 9
    • 77953909551 scopus 로고    scopus 로고
    • A self-assembly pathway to aligned monodomain gels
    • S. Zhang, and M.A. Greenfield S.I. Stupp A self-assembly pathway to aligned monodomain gels Nat. Mater. 9 2010 594 601
    • (2010) Nat. Mater. , vol.9 , pp. 594-601
    • Zhang, S.1    Greenfield, M.A.2    Stupp, S.I.3
  • 10
    • 39649085356 scopus 로고    scopus 로고
    • Temperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA16-I
    • Z. Ye, and H. Zhang X. Zhao Temperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA16-I J. Pept. Sci. 14 2008 152 162
    • (2008) J. Pept. Sci. , vol.14 , pp. 152-162
    • Ye, Z.1    Zhang, H.2    Zhao, X.3
  • 11
    • 0029064713 scopus 로고
    • Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides
    • H. Xiong, and B.L. Buckwalter M.H. Hecht 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 1995 6349 6353
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6349-6353
    • Xiong, H.1    Buckwalter, B.L.2    Hecht, M.H.3
  • 12
    • 67649998195 scopus 로고    scopus 로고
    • Effect of functionalization on the self-assembling propensity of β-sheet forming peptides
    • F. Taraballi, and M. Campione F. Gelain Effect of functionalization on the self-assembling propensity of β-sheet forming peptides Soft Matter 5 2009 660 668
    • (2009) Soft Matter , vol.5 , pp. 660-668
    • Taraballi, F.1    Campione, M.2    Gelain, F.3
  • 13
    • 0000590549 scopus 로고    scopus 로고
    • Left-handed helical ribbon intermediates in the self-assembly of a β-sheet peptide
    • D.M. Marini, and W. Hwang R.D. Kamm Left-handed helical ribbon intermediates in the self-assembly of a β-sheet peptide Nano Lett. 2 2002 295 299
    • (2002) Nano Lett. , vol.2 , pp. 295-299
    • Marini, D.M.1    Hwang, W.2    Kamm, R.D.3
  • 14
    • 77950350040 scopus 로고    scopus 로고
    • Fibrillar peptide gels in biotechnology and biomedicine
    • J.P. Jung, J.Z. Gasiorowski, and J.H. Collier Fibrillar peptide gels in biotechnology and biomedicine Biopolymers 94 2010 49 59
    • (2010) Biopolymers , vol.94 , pp. 49-59
    • Jung, J.P.1    Gasiorowski, J.Z.2    Collier, J.H.3
  • 15
    • 0027416047 scopus 로고
    • Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane
    • S. Zhang, and T. Holmes A. Rich Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane Proc. Natl. Acad. Sci. USA 90 1993 3334 3338
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3334-3338
    • Zhang, S.1    Holmes, T.2    Rich, A.3
  • 16
    • 0034612266 scopus 로고    scopus 로고
    • Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds
    • T.C. Holmes, and S. de Lacalle S. Zhang Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds Proc. Natl. Acad. Sci. USA 97 2000 6728 6733
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6728-6733
    • Holmes, T.C.1    De Lacalle, S.2    Zhang, S.3
  • 17
    • 54949097679 scopus 로고    scopus 로고
    • Designer self-assembling peptide nanofiber scaffolds for adult mouse neural stem cell 3-dimensional culture
    • F. Gelain, and D. Bottai S. Zhang Designer self-assembling peptide nanofiber scaffolds for adult mouse neural stem cell 3-dimensional culture PLoS One 1 2006 e119
    • (2006) PLoS One , vol.1 , pp. 119
    • Gelain, F.1    Bottai, D.2    Zhang, S.3
  • 18
    • 77957838631 scopus 로고    scopus 로고
    • The 3-D culture and in vivo growth of the human hepatocellular carcinoma cell line HepG2 in a self-assembling peptide nanofiber scaffold
    • M. Wu, and Z.H. Yang X. Zhao The 3-D culture and in vivo growth of the human hepatocellular carcinoma cell line HepG2 in a self-assembling peptide nanofiber scaffold J. Nanomater. 2010 2010 1 7
    • (2010) J. Nanomater. , vol.2010 , pp. 1-7
    • Wu, M.1    Yang, Z.H.2    Zhao, X.3
  • 19
    • 0037162463 scopus 로고    scopus 로고
    • Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: Implications for cartilage tissue repair
    • J. Kisiday, and M. Jin A.J. Grodzinsky Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: implications for cartilage tissue repair Proc. Natl. Acad. Sci. USA 99 2002 9996 10001
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9996-10001
    • Kisiday, J.1    Jin, M.2    Grodzinsky, A.J.3
  • 20
    • 14844338457 scopus 로고    scopus 로고
    • Self-assembling short oligopeptides and the promotion of angiogenesis
    • D.A. Narmoneva, and O. Oni R.T. Lee Self-assembling short oligopeptides and the promotion of angiogenesis Biomaterials 26 2005 4837 4846
    • (2005) Biomaterials , vol.26 , pp. 4837-4846
    • Narmoneva, D.A.1    Oni, O.2    Lee, R.T.3
  • 21
    • 18944376310 scopus 로고    scopus 로고
    • Topical palmitoyl pentapeptide provides improvement in photoaged human facial skin
    • L.R. Robinson, and N.C. Fitzgerald D.L. Bissett Topical palmitoyl pentapeptide provides improvement in photoaged human facial skin Int. J. Cosmet. Sci. 27 2005 155 160
    • (2005) Int. J. Cosmet. Sci. , vol.27 , pp. 155-160
    • Robinson, L.R.1    Fitzgerald, N.C.2    Bissett, D.L.3
  • 22
    • 24044468406 scopus 로고    scopus 로고
    • Membrane-mimetic nanocarriers formed by a dipalmitoylated cell-penetrating peptide
    • S. Keller, and I. Sauer M. Bienert Membrane-mimetic nanocarriers formed by a dipalmitoylated cell-penetrating peptide Angew. Chem. Int. Ed. Engl. 44 2005 5252 5255
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 5252-5255
    • Keller, S.1    Sauer, I.2    Bienert, M.3
  • 23
    • 44849089468 scopus 로고    scopus 로고
    • Sequence effect of self-assembling peptides on the complexation and in vitro delivery of the hydrophobic anticancer drug ellipticine
    • S.Y. Fung, H. Yang, and P. Chen Sequence effect of self-assembling peptides on the complexation and in vitro delivery of the hydrophobic anticancer drug ellipticine PLoS One 3 2008 e1956
    • (2008) PLoS One , vol.3 , pp. 1956
    • Fung, S.Y.1    Yang, H.2    Chen, P.3
  • 24
    • 3042537628 scopus 로고    scopus 로고
    • Biological surface engineering: A simple system for cell pattern formation
    • S. Zhang, and L. Yan A. Rich Biological surface engineering: a simple system for cell pattern formation Biomaterials 20 1999 1213 1220
    • (1999) Biomaterials , vol.20 , pp. 1213-1220
    • Zhang, S.1    Yan, L.2    Rich, A.3
  • 25
    • 0034621827 scopus 로고    scopus 로고
    • Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly
    • S.R. Whaley, and D.S. English A.M. Belcher Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly Nature 405 2000 665 668
    • (2000) Nature , vol.405 , pp. 665-668
    • Whaley, S.R.1    English, D.S.2    Belcher, A.M.3
  • 27
    • 20844451602 scopus 로고    scopus 로고
    • Dynamic reassembly of peptide RADA16 nanofiber scaffold
    • H. Yokoi, T. Kinoshita, and S. Zhang Dynamic reassembly of peptide RADA16 nanofiber scaffold Proc. Natl. Acad. Sci. USA 102 2005 8414 8419
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8414-8419
    • Yokoi, H.1    Kinoshita, T.2    Zhang, S.3
  • 30
    • 44049087105 scopus 로고    scopus 로고
    • The self-assembly, elasticity, and dynamics of cardiac thin filaments
    • M. Tassieri, and R.M.L. Evans T.A. Waigh The self-assembly, elasticity, and dynamics of cardiac thin filaments Biophys. J. 94 2008 2170 2178
    • (2008) Biophys. J. , vol.94 , pp. 2170-2178
    • Tassieri, M.1    Evans, R.M.L.2    Waigh, T.A.3
  • 31
    • 0022969835 scopus 로고
    • Structure and mobility of actin filaments as measured by quasielastic light scattering, viscometry, and electron microscopy
    • P.A. Janmey, and J. Peetermans T. Tanaka Structure and mobility of actin filaments as measured by quasielastic light scattering, viscometry, and electron microscopy J. Biol. Chem. 261 1986 8357 8362
    • (1986) J. Biol. Chem. , vol.261 , pp. 8357-8362
    • Janmey, P.A.1    Peetermans, J.2    Tanaka, T.3
  • 32
    • 0001921889 scopus 로고
    • Static light-scattering by aqueous-solutions of rodlike FD-virus particles
    • M. Hagenbuchle, and B. Weyerich R. Weber Static light-scattering by aqueous-solutions of rodlike FD-virus particles Physica A 169 1990 29 41
    • (1990) Physica A , vol.169 , pp. 29-41
    • Hagenbuchle, M.1    Weyerich, B.2    Weber, R.3
  • 34
    • 0034904210 scopus 로고    scopus 로고
    • Light scattering by fractal aggregates: A review
    • C.M. Sorensen Light scattering by fractal aggregates: a review Aerosol Sci. Technol. 35 2001 648 687
    • (2001) Aerosol Sci. Technol. , vol.35 , pp. 648-687
    • Sorensen, C.M.1
  • 35
    • 0037454218 scopus 로고    scopus 로고
    • Aggregation kinetics of polymer colloids in reaction limited regime: Experiments and simulations
    • M. Lattuada, and P. Sandkühler M. Morbidelli Aggregation kinetics of polymer colloids in reaction limited regime: experiments and simulations Adv. Colloid Interface Sci. 103 2003 33 56
    • (2003) Adv. Colloid Interface Sci. , vol.103 , pp. 33-56
    • Lattuada, M.1    Sandkühler, P.2    Morbidelli, M.3
  • 36
    • 0001146033 scopus 로고    scopus 로고
    • Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid beta-peptide
    • S.C. Jao, and K. Ma M.G. Zagorski Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid beta-peptide Amyloid: Int. J. Exp. Clin. Invest. 4 1997 240 252
    • (1997) Amyloid: Int. J. Exp. Clin. Invest. , vol.4 , pp. 240-252
    • Jao, S.C.1    Ma, K.2    Zagorski, M.G.3
  • 37
    • 4143071284 scopus 로고    scopus 로고
    • Self-assembly of the ionic peptide EAK16: The effect of charge distributions on self-assembly
    • S. Jun, and Y. Hong P. Chen Self-assembly of the ionic peptide EAK16: the effect of charge distributions on self-assembly Biophys. J. 87 2004 1249 1259
    • (2004) Biophys. J. , vol.87 , pp. 1249-1259
    • Jun, S.1    Hong, Y.2    Chen, P.3
  • 39
    • 26444450533 scopus 로고    scopus 로고
    • The effect of the mobile phase additives on sensitivity in the analysis of peptides and proteins by high-performance liquid chromatography-electrospray mass spectrometry
    • M.C. García The effect of the mobile phase additives on sensitivity in the analysis of peptides and proteins by high-performance liquid chromatography-electrospray mass spectrometry J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 825 2005 111 123
    • (2005) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.825 , pp. 111-123
    • García, M.C.1
  • 40
    • 0020857088 scopus 로고
    • Length dependence of rate constants for end-to-end association and dissociation of equilibrium linear aggregates
    • T.L. Hill Length dependence of rate constants for end-to-end association and dissociation of equilibrium linear aggregates Biophys. J. 44 1983 285 288
    • (1983) Biophys. J. , vol.44 , pp. 285-288
    • Hill, T.L.1
  • 41
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state
    • M.M. Pallitto, and R.M. Murphy A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state Biophys. J. 81 2001 1805 1822
    • (2001) Biophys. J. , vol.81 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 42
    • 0026708694 scopus 로고
    • Kinetics of aggregation of synthetic beta-amyloid peptide
    • S.J. Tomski, and R.M. Murphy Kinetics of aggregation of synthetic beta-amyloid peptide Arch. Biochem. Biophys. 294 1992 630 638
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 630-638
    • Tomski, S.J.1    Murphy, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.