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Biological and conformational studies on analogues of a synthetic peptide enhancing HIV‐1 infection
Author(s) -
Dettin Monica,
Scarinci Claudia,
Zanotto Carlo,
Roncon Rossella,
De Rossi Anita,
Di Bello Carlo
Publication year - 1998
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(199811)4:7<436::aid-psc163>3.0.co;2-c
Subject(s) - peptide , human immunodeficiency virus (hiv) , sequence (biology) , peptide sequence , biological activity , chemistry , glycoprotein , stereochemistry , function (biology) , biochemistry , in vitro , computational biology , combinatorial chemistry , biology , virology , microbiology and biotechnology , gene
We have previously demonstrated that a 23‐amino acid peptide derived from the V3 loop of the surface glycoprotein of the HIV‐1 strain MN is able to bind CD4 and to enhance HIV‐1 infection. Further studies have suggested that the peptide/CD4 interaction induces an increase in both CD4 expression and CD4/gp120 binding affinity. This paper describes the biological and physico‐chemical characterization of three analogues of reduced sequence that have been designed in order to identify the minimum active sequence of this peptide corresponding to the MN‐HIV‐1 principal neutralizing domain. Biological studies indicate that the entire sequence is required for biological activity and that the sequence 1–18 presents an inhibitory activity. CD and FT‐IR absorption data are discussed here in order to identify possible structure‐function correlations. © 1998 European Peptide Society and John Wiley & Sons, Ltd.