| Literature DB >> 24178885 |
G Vertuani1, M Boggian, A Breveglieri, G Cavicchioni, S Spisani, A Scatturin.
Abstract
In order to investigate the proper peptide backbone conformation able to elicit a biological activity, HCO-Met-Pro-Phe-OMe, HCO-Met-Ψ[COO]Leu-Phe-OMe, and HCO-Met-OLeu-Phe-OMe, analogues of the prototypical chemotactic peptide HCO-Met-Leu-Phe-OMe, were studied by CD and IR techniques. The results obtained comparing biological and conformational data evidence the critical presence of (i) the NH group at position 2, (ii) a rather flexible backbone, (iii) the chemical structure of the central residue which can affect the stability of a possible active conformer.Entities:
Year: 1995 PMID: 24178885 DOI: 10.1007/BF00807274
Source DB: PubMed Journal: Amino Acids ISSN: 0939-4451 Impact factor: 3.520