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The design of a specific ligand of HIV gp120
Author(s) -
Scarselli Maria,
Facchiano Antonio,
Russo Giandomenico,
Molinari Henriette,
Ragona Laura,
Zetta Lucia,
Niccolai Neri
Publication year - 1997
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199709)3:5<383::aid-psc123>3.0.co;2-c
Subject(s) - peptide , stereochemistry , chemistry , moiety , cysteine , cyclic peptide , ligand (biochemistry) , cystine , human immunodeficiency virus (hiv) , in vitro , sequence (biology) , biochemistry , receptor , biology , virology , enzyme
The crystal structure of CD4 suggested that the C/G 38 and C/L 44 replacements with the consequent cystine bridge formation are compatible with the native structure of that molecular moiety. As the NQGSF sequence, corresponding to the 39–43 fragment of human CD4 protein, was found to be involved in the HIV gp120 interaction, it has been synthesized in a cyclic form by adding two cysteine residues at the amino and carboxy termini. 1 H‐NMR studies show that the predominant solution conformation of cyclo‐[CNQGSFC] is a type II β‐turn centred on the NQGS segment. Structural and dynamic properties of the peptide are also analysed in relation to the in vitro activity. © 1997 European Peptide Society and John Wiley & Sons, Ltd. J. Pep. Sci. 3: 383–390 No. of Figures: 7. No. of Tables: 1. No. of References: 33.