Inhibition of /sup 125/I-labeled ristocetin binding to Micrococcus luteus cells by the peptides related to bacterial cell wall mucopeptide precursors: quantitative structure-activity relationships
Quantitative structure-activity relationships (QSAR) of N-Ac amino acids, N-Ac dipeptides, and N-Ac tripeptides in inhibition of /sup 125/I-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.
- Research Organization:
- Abbott Laboratories, Abbott Park, IL (USA)
- OSTI ID:
- 6397604
- Journal Information:
- J. Med. Chem.; (United States), Vol. 32:1
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
AMINO ACIDS
STRUCTURE-ACTIVITY RELATIONSHIPS
ANTIBIOTICS
BIOCHEMICAL REACTION KINETICS
PEPTIDES
ACETYLATION
CELL WALL
INHIBITION
IODINE 125
MICROCOCCUS
TRACER TECHNIQUES
ACYLATION
ANTI-INFECTIVE AGENTS
BACTERIA
BETA DECAY RADIOISOTOPES
CARBOXYLIC ACIDS
CELL CONSTITUENTS
CHEMICAL REACTIONS
DAYS LIVING RADIOISOTOPES
DRUGS
ELECTRON CAPTURE RADIOISOTOPES
INTERMEDIATE MASS NUCLEI
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
MICROORGANISMS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
RADIOISOTOPES
REACTION KINETICS
550201* - Biochemistry- Tracer Techniques