Structure-activity relationship of linear peptide Bu-His-DPhe-Arg-Trp-Gly-NH(2) at the human melanocortin-1 and -4 receptors: arginine substitution

A series of pentapeptides, based on Bu-His(6)-DPhe(7)-Arg(8)-Trp(9)-Gly(10)-NH(2) and modified at the Arg(8) position, was prepared and pharmacologically characterized. Peptides containing either cyanoguanidine or acylguanidine, two substantially less basic arginine surrogates, were found to retain...

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Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 2002-09, Vol.12 (17), p.2407-2410
Main Authors: Cheung, Adrian Wai-Hing, Danho, Waleed, Swistok, Joseph, Qi, Lida, Kurylko, Grazyna, Franco, Lucia, Yagaloff, Keith, Chen, Li
Format: Article
Language:English
Subjects:
Amino Acid Substitution
Arginine
Binding Sites
Guanidines
Humans
Oligopeptides - chemical synthesis
Oligopeptides - pharmacology
Protein Binding
Receptor, Melanocortin, Type 4
Receptors, Corticotropin - agonists
Receptors, Melanocortin
Structure-Activity Relationship
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Summary:A series of pentapeptides, based on Bu-His(6)-DPhe(7)-Arg(8)-Trp(9)-Gly(10)-NH(2) and modified at the Arg(8) position, was prepared and pharmacologically characterized. Peptides containing either cyanoguanidine or acylguanidine, two substantially less basic arginine surrogates, were found to retain the agonist activity of the parent peptide at both hMC1R and hMC4R. This study unequivocally shows that the positive charge of Arg(8) is not essential for efficient interactions of our pentapeptide with both hMC1R and hMC4R.
ISSN:0960-894X
1464-3405