메뉴 건너뛰기




Volumn 35, Issue 19, 2014, Pages 5196-5205

Coassembly of amphiphilic peptide EAK16-II with histidinylated analogues and implications for functionalization of β-sheet fibrils invivo

Author keywords

Amphiphilic peptides; Cross fibrils; EAK16; Protein formulation; Self assembly

Indexed keywords

IONIC STRENGTH; SELF ASSEMBLY;

EID: 84898454900     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2014.03.009     Document Type: Article
Times cited : (74)

References (28)
  • 1
    • 84872744450 scopus 로고    scopus 로고
    • Self-assembly for the synthesis of functional biomaterials
    • Stephanopoulos N., Ortony J.H., Stupp S.I. Self-assembly for the synthesis of functional biomaterials. Acta Mater 2013, 61:912-930.
    • (2013) Acta Mater , vol.61 , pp. 912-930
    • Stephanopoulos, N.1    Ortony, J.H.2    Stupp, S.I.3
  • 2
    • 60649096673 scopus 로고    scopus 로고
    • Self-assembling materials for therapeutic delivery
    • Branco M.C., Schneider J.P. Self-assembling materials for therapeutic delivery. Acta Biomater 2009, 5:817-831.
    • (2009) Acta Biomater , vol.5 , pp. 817-831
    • Branco, M.C.1    Schneider, J.P.2
  • 3
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • Zhang S. Fabrication of novel biomaterials through molecular self-assembly. Nat Biotechnol 2003, 21:1171-1178.
    • (2003) Nat Biotechnol , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 4
    • 19344363958 scopus 로고    scopus 로고
    • Self-assembly of ionic-complementary peptides: a physicochemical viewpoint
    • Chen P. Self-assembly of ionic-complementary peptides: a physicochemical viewpoint. Colloids Surf A Physicochem Eng Asp 2005, 261:3-24.
    • (2005) Colloids Surf A Physicochem Eng Asp , vol.261 , pp. 3-24
    • Chen, P.1
  • 5
    • 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
  • 6
    • 0034612266 scopus 로고    scopus 로고
    • Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds
    • Holmes T.C., de Lacalle S., Su X., Liu G., Rich A., Zhang S. Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds. Proc Natl Acad Sci U S A 2000, 97:6728-6733.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6728-6733
    • Holmes, T.C.1    de Lacalle, S.2    Su, X.3    Liu, G.4    Rich, A.5    Zhang, S.6
  • 7
    • 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
  • 8
    • 0029411957 scopus 로고
    • Self-complementary oligopeptide matrices support mammalian cell attachment
    • Zhang S., Holmes T.C., DiPersio C.M., Hynes R.O., Su X., Rich A. Self-complementary oligopeptide matrices support mammalian cell attachment. Biomaterials 1995, 16:1385-1393.
    • (1995) Biomaterials , vol.16 , pp. 1385-1393
    • Zhang, S.1    Holmes, T.C.2    DiPersio, C.M.3    Hynes, R.O.4    Su, X.5    Rich, A.6
  • 9
    • 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., Taraballi F., Natalello A., Villa O., et al. BMHP1-derived self-assembling peptides: hierarchically assembled structures with self-healing propensity and potential for tissue engineering applications. ACS Nano 2011, 5:1845-1859.
    • (2011) ACS Nano , vol.5 , pp. 1845-1859
    • Gelain, F.1    Silva, D.2    Caprini, A.3    Taraballi, F.4    Natalello, A.5    Villa, O.6
  • 13
    • 80053940876 scopus 로고    scopus 로고
    • Directed intermixing in multicomponent self-assembling biomaterials
    • Gasiorowski J.Z., Collier J.H. Directed intermixing in multicomponent self-assembling biomaterials. Biomacromolecules 2011, 12:3549-3558.
    • (2011) Biomacromolecules , vol.12 , pp. 3549-3558
    • Gasiorowski, J.Z.1    Collier, J.H.2
  • 14
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure fromcircular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTRmethods with an expanded reference set
    • Sreerama N., Woody R.W. Estimation of protein secondary structure fromcircular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTRmethods with an expanded reference set. Anal Biochem 2000, 287:252-260.
    • (2000) Anal Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 15
    • 0037699014 scopus 로고    scopus 로고
    • Concentration effect on the aggregation of a self-assembling oligopeptide
    • Fung S.Y., Keyes C., Duhamel J., Chen P. Concentration effect on the aggregation of a self-assembling oligopeptide. Biophys J 2003, 85:537-548.
    • (2003) Biophys J , vol.85 , pp. 537-548
    • Fung, S.Y.1    Keyes, C.2    Duhamel, J.3    Chen, P.4
  • 16
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with thioflavin T
    • LeVine H. Quantification of β-sheet amyloid fibril structures with thioflavin T. Meth Enzymol 1999, 309:274-284.
    • (1999) Meth Enzymol , vol.309 , pp. 274-284
    • LeVine, H.1
  • 17
    • 0031574012 scopus 로고    scopus 로고
    • Conformation of β-lactoglobulin studied by FTIR: effect of pH, temperature, and adsorption to the oil-water interface
    • Fang Y., Dalgleish D.G. Conformation of β-lactoglobulin studied by FTIR: effect of pH, temperature, and adsorption to the oil-water interface. JColloid Interface Sci 1997, 196:292-298.
    • (1997) JColloid Interface Sci , vol.196 , pp. 292-298
    • Fang, Y.1    Dalgleish, D.G.2
  • 18
    • 33745384433 scopus 로고    scopus 로고
    • FTIR and nDSC as analytical tools for high-concentration protein formulations
    • Matheus S., Friess W., Mahler H.-C. FTIR and nDSC as analytical tools for high-concentration protein formulations. Pharm Res 2006, 23:1350-1363.
    • (2006) Pharm Res , vol.23 , pp. 1350-1363
    • Matheus, S.1    Friess, W.2    Mahler, H.-C.3
  • 19
    • 0141483558 scopus 로고    scopus 로고
    • Effect of amino acid sequence and pH on nanofiber formation of self-assembling peptides EAK16-II and EAK16-IV
    • Hong Y., Legge R.L., Zhang S., Chen P. Effect of amino acid sequence and pH on nanofiber formation of self-assembling peptides EAK16-II and EAK16-IV. Biomacromolecules 2003, 4:1433-1442.
    • (2003) Biomacromolecules , vol.4 , pp. 1433-1442
    • Hong, Y.1    Legge, R.L.2    Zhang, S.3    Chen, P.4
  • 20
    • 28944434118 scopus 로고    scopus 로고
    • Effect of NaCl and peptide concentration on the self-assembly of an ionic-complementary peptide EAK16-II
    • Hong Y., Pritzker M.D., Legge R.L., Chen P. Effect of NaCl and peptide concentration on the self-assembly of an ionic-complementary peptide EAK16-II. Colloids Surf B Biointerfaces 2005, 46:152-161.
    • (2005) Colloids Surf B Biointerfaces , vol.46 , pp. 152-161
    • Hong, Y.1    Pritzker, M.D.2    Legge, R.L.3    Chen, P.4
  • 21
    • 62749099087 scopus 로고    scopus 로고
    • Overlooking subvisible particles in therapeutic protein products: gaps that may compromise product quality
    • Carpenter J.F., Randolph T.W., Jiskoot W., Crommelin D.J., Middaugh C.R., Winter G., et al. Overlooking subvisible particles in therapeutic protein products: gaps that may compromise product quality. JPharm Sci 2009, 98:1201-1205.
    • (2009) JPharm Sci , vol.98 , pp. 1201-1205
    • Carpenter, J.F.1    Randolph, T.W.2    Jiskoot, W.3    Crommelin, D.J.4    Middaugh, C.R.5    Winter, G.6
  • 22
    • 0027524623 scopus 로고
    • Charged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone charges
    • Armstrong K.M., Baldwin R.L. Charged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone charges. Proc Natl Acad Sci U S A 1993, 90:11337-11340.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 11337-11340
    • Armstrong, K.M.1    Baldwin, R.L.2
  • 23
    • 0026608073 scopus 로고
    • Environment affects amino acid preference for secondary structure
    • Zhong L., Johnson W.C. Environment affects amino acid preference for secondary structure. Proc Natl Acad Sci U S A 1992, 89:4462-4465.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 4462-4465
    • Zhong, L.1    Johnson, W.C.2
  • 24
    • 0034584899 scopus 로고    scopus 로고
    • Proteins that convert from a helix to b sheet implications for folding and disease
    • Gro B.M. Proteins that convert from a helix to b sheet implications for folding and disease. Curr Protein Pept Sci 2000, 1:339-347.
    • (2000) Curr Protein Pept Sci , vol.1 , pp. 339-347
    • Gro, B.M.1
  • 25
    • 0025276149 scopus 로고
    • Peptides as conformational switch: medium-induced conformational transitions of designed peptides
    • Mutter M., Hersperger R. Peptides as conformational switch: medium-induced conformational transitions of designed peptides. Angew Chem Int Ed Engl 1990, 29:185-187.
    • (1990) Angew Chem Int Ed Engl , vol.29 , pp. 185-187
    • Mutter, M.1    Hersperger, R.2
  • 26
    • 33644854942 scopus 로고    scopus 로고
    • Gerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" model
    • Gobbi M., Colombo L., Morbin M., Mazzoleni G., Accardo E., Vanoni M., et al. Gerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" model. JBiol Chem 2006, 281:843-849.
    • (2006) JBiol Chem , vol.281 , pp. 843-849
    • Gobbi, M.1    Colombo, L.2    Morbin, M.3    Mazzoleni, G.4    Accardo, E.5    Vanoni, M.6
  • 27
    • 48749090708 scopus 로고    scopus 로고
    • Conformational plasticity of the Gerstmann-Sträussler-Scheinker disease peptide as indicated by its multiple aggregation pathways
    • Natalello A., Prokorov V.V., Tagliavini F., Morbin M., Forloni G., Beeg M., et al. Conformational plasticity of the Gerstmann-Sträussler-Scheinker disease peptide as indicated by its multiple aggregation pathways. JMol Biol 2008, 381:1349-1361.
    • (2008) JMol Biol , vol.381 , pp. 1349-1361
    • Natalello, A.1    Prokorov, V.V.2    Tagliavini, F.3    Morbin, M.4    Forloni, G.5    Beeg, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.