Conformational analysis of tripeptide Ac-Lys-Pro-Val-NH2, COOH-terminal sequence of alpha-MSH

Alpha‐melanocyte stimulating hormone (alpha‐MSH) is an endogenous linear tridecapeptide which interacts with the melanocortin receptors (MC1‐R to MC5‐R) to mediate its biological effects. Antipyretic and anti‐inflammatory activities of alpha‐MSH are due to the COOH‐terminal peptide sequence, Lys‐Pro...

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Bibliographic Details
Published in:Journal of pharmacy and pharmacology 2001-07, Vol.53 (7), p.949-953
Main Authors: Chavatte, Philippe, Yous, Saïd, Lesieur, Daniel, Hénichar, Jean-Pierre
Format: Article
Language:English
Subjects:
Biological and medical sciences
Bones, joints and connective tissue. Antiinflammatory agents
Computer Simulation
Medical sciences
Melanocyte-Stimulating Hormones - chemistry
Models, Molecular
Peptide Fragments - chemistry
Pharmacology. Drug treatments
Protein Conformation
Software
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Summary:Alpha‐melanocyte stimulating hormone (alpha‐MSH) is an endogenous linear tridecapeptide which interacts with the melanocortin receptors (MC1‐R to MC5‐R) to mediate its biological effects. Antipyretic and anti‐inflammatory activities of alpha‐MSH are due to the COOH‐terminal peptide sequence, Lys‐Pro‐Val (alpha‐MSH[11–13]). This tripeptide might be useful as a therapeutic agent in the control of fever and inflammatory reactions. With this aim, a theoretical conformational study of the tripeptide has been carried out using molecular dynamics. The obtained conformational space has been classified into families according to the letter‐code convention to partition the φ‐ψ map. The lowest energy conformations of each family were used as templates to design six models of conformationally constrained non‐peptide analogues.
ISSN:0022-3573
2042-7158
DOI:10.1211/0022357011776360