In:
Journal of Peptide Science, Wiley, Vol. 13, No. 6 ( 2007-06), p. 413-421
Abstract:
Peptide T (ASTTTNYT), a segment corresponding to residues 185–192 of gp120, the coat protein of HIV, has several important biological properties in vitro that have stimulated the search for simpler and possibly more active analogs. We have previously shown that pseudocyclic hexapeptide analogs containing the central residues of peptide T retain considerable chemotactic activity. We have now extended the design of this type of analogs to peptides containing different aromatic residues and/or Ser in lieu of Thr. The complex conformation‐activity relationship of these analogs called for a reexamination of the basic conformational tendencies of peptide T itself. Here, we present an exhaustive NMR conformational study of peptide T in different media. Peptide T assumes a γ‐turn in aqueous mixtures of ethylene glycol, a type‐IV β‐turn conformation in aqueous mixtures of DMF, and a type‐II β‐turn conformation in aqueous mixtures of DMSO. The preferred conformations for the analogs were derived from modeling, starting from the preferred conformations of peptide T. The best models derived from the γ‐turn conformation of peptide T are those of peptides XII (DSNYSR), XIII (ETNYTK) and XVI (ESNYSR). The best models derived from the type‐IV β‐turn conformation of peptide T are those of peptides XIV (KTTNYE) and XV (DSSNYR). No low‐energy models could be derived starting from the type‐II β‐turn conformation of peptide T. The analogs with the most favored conformations are also the most active in the chemotactic test. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.
Type of Medium:
Online Resource
ISSN:
1075-2617
,
1099-1387
Language:
English
Publisher:
Wiley
Publication Date:
2007
detail.hit.zdb_id:
1491819-5
SSG:
12
