Structure-activity relationship study of CXCR4 antagonists bearing the cyclic pentapeptide scaffold: identification of the new pharmacophore

A highly potent CXCR4 antagonist 2 [cyclo (-D-Tyr1-Arg2-Arg3-Nal4-Gly5-)] has previously been identified by screening cyclic pentapeptide libraries that were designed based on pharmacophore residues of a 14-residue peptidic CXCR4 antagonist 1. In the present study, D-Tyr and Arg in peptide 2 were re...

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Bibliographic Details
Published in:Organic & biomolecular chemistry 2008-01, Vol.6 (23), p.4374
Main Authors: Tanaka, Tomohiro, Tsutsumi, Hiroshi, Nomura, Wataru, Tanabe, Yasuaki, Ohashi, Nami, Esaka, Ai, Ochiai, Chihiro, Sato, Jun, Itotani, Kyoko, Murakami, Tsutomu, Ohba, Kenji, Yamamoto, Naoki, Fujii, Nobutaka, Tamamura, Hirokazu
Format: Article
Language:English
Subjects:
Animals
Cattle
Cell Line
Drug Discovery
HIV-1 - drug effects
Humans
Oligopeptides - chemical synthesis
Oligopeptides - chemistry
Oligopeptides - pharmacology
Oligopeptides - toxicity
Peptides, Cyclic - chemical synthesis
Peptides, Cyclic - chemistry
Peptides, Cyclic - pharmacology
Peptides, Cyclic - toxicity
Receptors, CXCR4 - antagonists & inhibitors
Structure-Activity Relationship
Tyrosine - chemistry
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Summary:A highly potent CXCR4 antagonist 2 [cyclo (-D-Tyr1-Arg2-Arg3-Nal4-Gly5-)] has previously been identified by screening cyclic pentapeptide libraries that were designed based on pharmacophore residues of a 14-residue peptidic CXCR4 antagonist 1. In the present study, D-Tyr and Arg in peptide 2 were replaced by a bicyclic aromatic amino acid and a cationic amino acid, respectively, and their binding activity for CXCR4 was evaluated for identification of the novel pharmacophore.
ISSN:1477-0520
1477-0539
DOI:10.1039/b812029c