title: Inhibition of 125I-labeled ristocetin binding to Micrococcus luteus cells by the peptides related to bacterial cell wall mucopeptide precursors: quantitative structure-activity relationships.
abstract: Quantitative structure-activity relationships (QSAR) of N-Ac amino acids, N-Ac dipeptides, and N-Ac tripeptides in inhibition of 125I-labeled ristocetin binding to Micrococcus luteus cell wall have been developed to probe the details of the binding between ristocetin and N-acetylated peptides. The correlation equations indicate that (1) the binding is stronger for peptides in which the side chain of the C-terminal amino acid has a large molar refractivity (MR) value, (2) the binding is weaker for peptides with polar than for those with nonpolar C-terminal side chains, (3) the N-terminal amino acid in N-Ac dipeptides contributes 12 times that of the C-terminal amino acid to binding affinity, and (4) the interactions between ristocetin and the N-terminal amino acid of N-acetyl tripeptides appear to be much weaker than those with the first two amino acids.
authors.affiliation: Pharmaceutical Products Division, Abbott Laboratories, Abbott Park, Illinois 60064.
authors.forename: K H
authors.initials: KH
authors.lastname: Kim
authors.forename: Y
authors.initials: Y
authors.lastname: Martin
authors.forename: E
authors.initials: E
authors.lastname: Otis
authors.forename: J
authors.initials: J
authors.lastname: Mao
mesh_terms: D000107:Acetylation; D001667:Binding, Competitive; D002473:Cell Wall / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D007457:Iodine Radioisotopes; D008837:Micrococcus / Q000378:metabolism*; D008958:Models, Molecular; D009842:Oligopeptides / Q000378:metabolism*; D011869:Radioligand Assay; D012310:Ristocetin / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D007457:Iodine Radioisotopes; D009842:Oligopeptides; D012310:Ristocetin