Structure-activity relationship study on artificial CXCR4 ligands possessing the cyclic pentapeptide scaffold: the exploration of amino acid residues of pentapeptides by substitutions of several aromatic amino acids.

Authors

• Tomohiro Tanaka
• Wataru Nomura
• Tetsuo Narumi
• Ai Esaka
• Shinya Oishi
• Nami Ohashi
• Kyoko Itotani
• Barry J Evans
• Zi-xuan Wang
• Stephen C Peiper
• Nobutaka Fujii
• Hirokazu Tamamura

Publication/Presentation Date

9-21-2009

Abstract

Previously, downsizing of a 14-residue peptidic CXCR4 antagonist has led to the development of a highly potent CXCR4 antagonist [cyclo(-d-Tyr(1)-Arg(2)-Arg(3)-Nal(4)-Gly(5)-)]. In the present study, cyclic pentapeptide libraries that were designed by substitutions of several amino acids for d-Tyr(1) and Arg(2) in peptide were prepared and screened to evaluate binding activity for CXCR4. The above structure-activity relationship study led to the finding of several potent CXCR4 ligands.

Volume

7

Issue

18

First Page

3805

Last Page

3809

ISSN

1477-0539

Published In/Presented At

Tanaka, T., Nomura, W., Narumi, T., Esaka, A., Oishi, S., Ohashi, N., Itotani, K., Evans, B. J., Wang, Z. X., Peiper, S. C., Fujii, N., & Tamamura, H. (2009). Structure-activity relationship study on artificial CXCR4 ligands possessing the cyclic pentapeptide scaffold: the exploration of amino acid residues of pentapeptides by substitutions of several aromatic amino acids. Organic & biomolecular chemistry, 7(18), 3805–3809. https://doi.org/10.1039/b908286g

Disciplines

Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods

PubMedID

19707686

Department(s)

Administration and Leadership

Document Type

Article