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Volumn 118, Issue 25, 1996, Pages 5836-5845

A 2,3'-substituted biphenyl-based amino acid facilitates the formation of a monomeric β-hairpin-like structure in aqueous solution at elevated temperature

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; BIPHENYL DERIVATIVE; SYNTHETIC PEPTIDE;

EID: 0030037714     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja952472x     Document Type: Article
Times cited : (72)

References (121)
  • 47
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    • Several small peptides are capable of populating a β-turn conformation; see: (a) Rose, G. D.; Gierasch, L. M.; Smith, J. A. Adv. Protein Chem. 1985, 17, 1-109. (b) Rizo, J.; Gierasch, L. M. Annu. Rev. Biochem. 1992, 61, 387-418. (c) Dyson, H. J.; Cross, K. J.; Houghten, R. A.; Wilson, I. A.; Wright, P. E.; Lerner, R. A. Nature 1985, 318, 480. (d) Hruby, V. J. In Chemistry and Biochemistry of Amino Acids; Weinstein, B., Ed.; M. Dekker: New York, 1974; Vol. 3, pp 1-188. (e) Hruby, V. J.; Al-Obeidi, F.; Kazmierski, W. Biochem. J. 1990, 268, 249-262. (f) Hruby, V. J. Life Sci. 1982, 31, 189-199. However, concensus β-turn sequences do not appear to be sufficient to nucleate folding within sequences which are known to fold when nucleated by unnatural amino acids such as the 4-(2-aminoethyl)-6-dibenzofuranpropionic acid, unpublished results.
    • (1985) Adv. Protein Chem. , vol.17 , pp. 1-109
    • Rose, G.D.1    Gierasch, L.M.2    Smith, J.A.3
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    • Several small peptides are capable of populating a β-turn conformation; see: (a) Rose, G. D.; Gierasch, L. M.; Smith, J. A. Adv. Protein Chem. 1985, 17, 1-109. (b) Rizo, J.; Gierasch, L. M. Annu. Rev. Biochem. 1992, 61, 387-418. (c) Dyson, H. J.; Cross, K. J.; Houghten, R. A.; Wilson, I. A.; Wright, P. E.; Lerner, R. A. Nature 1985, 318, 480. (d) Hruby, V. J. In Chemistry and Biochemistry of Amino Acids; Weinstein, B., Ed.; M. Dekker: New York, 1974; Vol. 3, pp 1-188. (e) Hruby, V. J.; Al-Obeidi, F.; Kazmierski, W. Biochem. J. 1990, 268, 249-262. (f) Hruby, V. J. Life Sci. 1982, 31, 189-199. However, concensus β-turn sequences do not appear to be sufficient to nucleate folding within sequences which are known to fold when nucleated by unnatural amino acids such as the 4-(2-aminoethyl)-6-dibenzofuranpropionic acid, unpublished results.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 387-418
    • Rizo, J.1    Gierasch, L.M.2
  • 49
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    • Several small peptides are capable of populating a β-turn conformation; see: (a) Rose, G. D.; Gierasch, L. M.; Smith, J. A. Adv. Protein Chem. 1985, 17, 1-109. (b) Rizo, J.; Gierasch, L. M. Annu. Rev. Biochem. 1992, 61, 387-418. (c) Dyson, H. J.; Cross, K. J.; Houghten, R. A.; Wilson, I. A.; Wright, P. E.; Lerner, R. A. Nature 1985, 318, 480. (d) Hruby, V. J. In Chemistry and Biochemistry of Amino Acids; Weinstein, B., Ed.; M. Dekker: New York, 1974; Vol. 3, pp 1-188. (e) Hruby, V. J.; Al-Obeidi, F.; Kazmierski, W. Biochem. J. 1990, 268, 249-262. (f) Hruby, V. J. Life Sci. 1982, 31, 189-199. However, concensus β-turn sequences do not appear to be sufficient to nucleate folding within sequences which are known to fold when nucleated by unnatural amino acids such as the 4-(2-aminoethyl)-6-dibenzofuranpropionic acid, unpublished results.
    • (1985) Nature , vol.318 , pp. 480
    • Dyson, H.J.1    Cross, K.J.2    Houghten, R.A.3    Wilson, I.A.4    Wright, P.E.5    Lerner, R.A.6
  • 50
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    • Weinstein, B., Ed.; M. Dekker: New York
    • Several small peptides are capable of populating a β-turn conformation; see: (a) Rose, G. D.; Gierasch, L. M.; Smith, J. A. Adv. Protein Chem. 1985, 17, 1-109. (b) Rizo, J.; Gierasch, L. M. Annu. Rev. Biochem. 1992, 61, 387-418. (c) Dyson, H. J.; Cross, K. J.; Houghten, R. A.; Wilson, I. A.; Wright, P. E.; Lerner, R. A. Nature 1985, 318, 480. (d) Hruby, V. J. In Chemistry and Biochemistry of Amino Acids; Weinstein, B., Ed.; M. Dekker: New York, 1974; Vol. 3, pp 1-188. (e) Hruby, V. J.; Al-Obeidi, F.; Kazmierski, W. Biochem. J. 1990, 268, 249-262. (f) Hruby, V. J. Life Sci. 1982, 31, 189-199. However, concensus β-turn sequences do not appear to be sufficient to nucleate folding within sequences which are known to fold when nucleated by unnatural amino acids such as the 4-(2-aminoethyl)-6-dibenzofuranpropionic acid, unpublished results.
    • (1974) Chemistry and Biochemistry of Amino Acids , vol.3 , pp. 1-188
    • Hruby, V.J.1
  • 51
    • 0025336463 scopus 로고
    • Several small peptides are capable of populating a β-turn conformation; see: (a) Rose, G. D.; Gierasch, L. M.; Smith, J. A. Adv. Protein Chem. 1985, 17, 1-109. (b) Rizo, J.; Gierasch, L. M. Annu. Rev. Biochem. 1992, 61, 387-418. (c) Dyson, H. J.; Cross, K. J.; Houghten, R. A.; Wilson, I. A.; Wright, P. E.; Lerner, R. A. Nature 1985, 318, 480. (d) Hruby, V. J. In Chemistry and Biochemistry of Amino Acids; Weinstein, B., Ed.; M. Dekker: New York, 1974; Vol. 3, pp 1-188. (e) Hruby, V. J.; Al-Obeidi, F.; Kazmierski, W. Biochem. J. 1990, 268, 249-262. (f) Hruby, V. J. Life Sci. 1982, 31, 189-199. However, concensus β-turn sequences do not appear to be sufficient to nucleate folding within sequences which are known to fold when nucleated by unnatural amino acids such as the 4-(2-aminoethyl)-6-dibenzofuranpropionic acid, unpublished results.
    • (1990) Biochem. J. , vol.268 , pp. 249-262
    • Hruby, V.J.1    Al-Obeidi, F.2    Kazmierski, W.3
  • 52
    • 0019958979 scopus 로고
    • Several small peptides are capable of populating a β-turn conformation; see: (a) Rose, G. D.; Gierasch, L. M.; Smith, J. A. Adv. Protein Chem. 1985, 17, 1-109. (b) Rizo, J.; Gierasch, L. M. Annu. Rev. Biochem. 1992, 61, 387-418. (c) Dyson, H. J.; Cross, K. J.; Houghten, R. A.; Wilson, I. A.; Wright, P. E.; Lerner, R. A. Nature 1985, 318, 480. (d) Hruby, V. J. In Chemistry and Biochemistry of Amino Acids; Weinstein, B., Ed.; M. Dekker: New York, 1974; Vol. 3, pp 1-188. (e) Hruby, V. J.; Al-Obeidi, F.; Kazmierski, W. Biochem. J. 1990, 268, 249-262. (f) Hruby, V. J. Life Sci. 1982, 31, 189-199. However, concensus β-turn sequences do not appear to be sufficient to nucleate folding within sequences which are known to fold when nucleated by unnatural amino acids such as the 4-(2-aminoethyl)-6-dibenzofuranpropionic acid, unpublished results.
    • (1982) Life Sci. , vol.31 , pp. 189-199
    • Hruby, V.J.1
  • 79
  • 103
    • 8944233381 scopus 로고    scopus 로고
    • note
    • The higher concentration of peptide E (0.20 mM) versus peptide D (0.15 mM) in these studies increases the likelihood of stabilizing an intramolecular sheet by self-assembly. However, no structure is observed over the pH range of 4-9.8, providing strong evidence that peptide E does not form intramolecular β-sheet structure under these conditions.
  • 104
    • 8944229710 scopus 로고    scopus 로고
    • note
    • 3 group of Leu-3 in peptide A and Leu-6 in peptide E was also observed. The significant increase in upfield shifting (0.3 ppm relative to that of the remaining valine methyl groups) suggests the presence of a closer interaction between the leucine δ′-methyl group and one of the aromatic rings of the biphenyl system.
  • 121
    • 0001339532 scopus 로고
    • This figure was prepared with MolScript; see: Kraulis, P. T. J. Appl. Crystallogr. 1991, 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.