메뉴 건너뛰기




Volumn 35, Issue 2, 2006, Pages 162-169

Probing the importance of lateral hydrophobic association in self-assembling peptide hydrogelators

Author keywords

Design; Hydrogel; Peptide; Self assembly; Tissue engineering; Viscoelastic

Indexed keywords

NANOPARTICLE; PEPTIDE;

EID: 29944436353     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-005-0017-7     Document Type: Article
Times cited : (73)

References (24)
  • 2
    • 0000790964 scopus 로고    scopus 로고
    • Molecular tailoring of thermoreversible copolymer gels: Some new mechanistic insights
    • Badiger MV, Lele AK, Bhalerao VS, Varghese S, Mashelkar RA (1998) Molecular tailoring of thermoreversible copolymer gels: Some new mechanistic insights. J Chem Phy 109:1175-1184
    • (1998) J Chem Phy , vol.109 , pp. 1175-1184
    • Badiger, M.V.1    Lele, A.K.2    Bhalerao, V.S.3    Varghese, S.4    Mashelkar, R.A.5
  • 3
    • 0000325130 scopus 로고
    • Pro-D-NMe-Amino Acid and D-Pro-NMe-Amino Acid: Simple, efficient reverse-turn constraints
    • Chalmers DK, Marshall GR (1995) Pro-D-NMe-Amino Acid and D-Pro-NMe-Amino Acid: simple, efficient reverse-turn constraints. J Am Chem Soc 117:5927-5937
    • (1995) J Am Chem Soc , vol.117 , pp. 5927-5937
    • Chalmers, D.K.1    Marshall, G.R.2
  • 5
    • 0033620414 scopus 로고    scopus 로고
    • Structural mimicry of canonical conformations in antibody hypervariable loops using cyclic peptides containing a heterochiral diproline template
    • Favre M, Moehle K, Jiang L, Pfeifler B, Robinson JA (1999) Structural mimicry of canonical conformations in antibody hypervariable loops using cyclic peptides containing a heterochiral diproline template. J Am Chem Soc 121:2679-2685
    • (1999) J Am Chem Soc , vol.121 , pp. 2679-2685
    • Favre, M.1    Moehle, K.2    Jiang, L.3    Pfeifler, B.4    Robinson, J.A.5
  • 6
    • 0031455857 scopus 로고    scopus 로고
    • b-hairpins in proteins revisited: Lessons for de novo design
    • Gunasekaran K, Ramakrishnan C, Balaram P (1997) b-hairpins in proteins revisited: lessons for de novo design. Protein Eng 10:1131-1141
    • (1997) Protein Eng , vol.10 , pp. 1131-1141
    • Gunasekaran, K.1    Ramakrishnan, C.2    Balaram, P.3
  • 7
    • 0036139571 scopus 로고    scopus 로고
    • Novel peptide-based biomaterial scaffolds for tissue engineering
    • Holmes TC (2002) Novel peptide-based biomaterial scaffolds for tissue engineering. Trends in Biotech 20:16-21
    • (2002) Trends in Biotech , vol.20 , pp. 16-21
    • Holmes, T.C.1
  • 8
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • Hutchinson EG, Thornton JM (1994) A revised set of potentials for beta-turn formation in proteins. Prot Science 3:2207-2216
    • (1994) Prot Science , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 10
    • 0037864443 scopus 로고    scopus 로고
    • Design and application of basic amino acids displaying enhanced hydrophobicity
    • Kretsinger JK, Schneider JP (2003) Design and application of basic amino acids displaying enhanced hydrophobicity. J Am Chem Soc 125:7907-7913
    • (2003) J Am Chem Soc , vol.125 , pp. 7907-7913
    • Kretsinger, J.K.1    Schneider, J.P.2
  • 11
    • 0035385135 scopus 로고    scopus 로고
    • Hydrogels for tissue engineering
    • Lee KY, Mooney DJ (2001) Hydrogels for tissue engineering. Chem Rev 101:1869-1879
    • (2001) Chem Rev , vol.101 , pp. 1869-1879
    • Lee, K.Y.1    Mooney, D.J.2
  • 12
    • 0025098571 scopus 로고
    • Common features of protein unfolding and dissolution of hydrophobic compounds
    • Murphy KP, Privalov PL, Gill SJ (1990) Common features of protein unfolding and dissolution of hydrophobic compounds. Science 247:559-561
    • (1990) Science , vol.247 , pp. 559-561
    • Murphy, K.P.1    Privalov, P.L.2    Gill, S.J.3
  • 13
    • 0007912674 scopus 로고
    • X-ray crystal structure of pivaloyl-D-pro-L-pro-L-ala-N-methylamide; observation of a consecutive b-turn conformation
    • Nair CM, Vijayan M, Venkatachalapathi YV, Balaram P (1979) X-ray crystal structure of pivaloyl-D-pro-L-pro-L-ala-N-methylamide; observation of a consecutive b-turn conformation. J Chem Soc, Chem Commun pp 1183-1184
    • (1979) J Chem Soc, Chem Commun , pp. 1183-1184
    • Nair, C.M.1    Vijayan, M.2    Venkatachalapathi, Y.V.3    Balaram, P.4
  • 14
    • 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 (2004a) Salt-triggered peptide folding and consequent self-assembly into hydrogels with tunable modulus. Macromolecules 37:7331-7337
    • (2004) Macromolecules , vol.37 , pp. 7331-7337
    • Ozbas, B.1    Kretsinger, J.2    Rajagopal, K.3    Schneider, J.P.4    Pochan, D.J.5
  • 15
    • 42749104107 scopus 로고    scopus 로고
    • Semi-flexible chain networks formed via self-assembly of b-hairpin molecules
    • Ozbas B, Rajagopal K, Schneider JP, Pochan DJ (2004b) Semi-flexible chain networks formed via self-assembly of b-hairpin molecules. Phys Rev Letters 93:268106/268101-268106/268104
    • (2004) Phys Rev Letters , vol.93
    • Ozbas, B.1    Rajagopal, K.2    Schneider, J.P.3    Pochan, D.J.4
  • 16
    • 0141596163 scopus 로고    scopus 로고
    • Thermally reversible hydrogels via intramolecular folding and consequent self-assembly of a de novo designed peptide
    • Pochan DJ, Schneider JP, Kretsinger J, Ozbas B, Rajagopal K, Haines L (2003) Thermally reversible hydrogels via intramolecular folding and consequent self-assembly of a de novo designed peptide. J Am Chem Soc 125:11802-11803
    • (2003) J Am Chem Soc , vol.125 , pp. 11802-11803
    • Pochan, D.J.1    Schneider, J.P.2    Kretsinger, J.3    Ozbas, B.4    Rajagopal, K.5    Haines, L.6
  • 17
    • 0141747446 scopus 로고
    • Stability of protein-structure and hydrophobic interactions
    • Privalov PL (1988) Stability of protein-structure and hydrophobic interactions. Biol Chem Hoppe-Seyler 369:199
    • (1988) Biol Chem Hoppe-Seyler , vol.369 , pp. 199
    • Privalov, P.L.1
  • 19
    • 4143141192 scopus 로고    scopus 로고
    • Self-assembling peptides and proteins for nanotechnological applications
    • Rajagopal K, Schneider JP (2004) Self-assembling peptides and proteins for nanotechnological applications. Curr Opin Struct Biol 14:480-486
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 480-486
    • Rajagopal, K.1    Schneider, J.P.2
  • 20
  • 21
    • 0027339355 scopus 로고
    • Accommodating sequence changes in b-hairpin in proteins
    • Sibanda B, Thornton JM (1993) Accommodating sequence changes in b-hairpin in proteins. J Mol Biol 229:428-447
    • (1993) J Mol Biol , vol.229 , pp. 428-447
    • Sibanda, B.1    Thornton, J.M.2
  • 22
    • 0021844602 scopus 로고
    • b-Hairpin families in globular proteins
    • Sibanda BL, Thornton JM (1985) b-Hairpin families in globular proteins. Nature 316:170-176
    • (1985) Nature , vol.316 , pp. 170-176
    • Sibanda, B.L.1    Thornton, J.M.2
  • 23
    • 0029058159 scopus 로고
    • An analysis of side-chain interactions and pair correlations within antiparallel beta-sheets - The differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs
    • Wouters MA, Curmi PMG (1995) An analysis of side-chain interactions and pair correlations within antiparallel beta-sheets - the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs. Proteins-Struct Functi Geneti 22:119-131
    • (1995) Proteins-Struct Functi Geneti , vol.22 , pp. 119-131
    • Wouters, M.A.1    Curmi, P.M.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.