Peptide inhibitors of CDK2-cyclin A that target the cyclin recruitment-Site: Structural variants of the C-Terminal Phe

Atkinson, Gail E.; Cowan, Angela; McInnes, Campbell; Zheleva, Daniella I.; Fischer, Peter M.; Chan, Weng C.

Abstract

A focused series of octapeptides based on the lead compound H-His-Ala-Lys-Arg-Arg-Leu-Ile-Phe-NH2 1, in which the C-terminal phenylalanine residue was replaced by α and/or β-modified variants, was synthesized using solid-phase chemistry. Both the L-threo-β-hydroxy-phenylalanine (β-phenylserine, Pse) and (2S)-phenylalaninol derivatives, as competitive binders at the cyclin-recruitment site, displayed potent inhibitory activity towards the CDK2-cyclin A complex. Unexpectedly, the D-threo-Pse derivatives also showed inhibitory activity. © 2002 Elsevier Science Ltd. All rights reserved.

Citation

Atkinson, G. E., Cowan, A., McInnes, C., Zheleva, D. I., Fischer, P. M., & Chan, W. C. (2002). Peptide inhibitors of CDK2-cyclin A that target the cyclin recruitment-Site: Structural variants of the C-Terminal Phe. Bioorganic and Medicinal Chemistry Letters, 12(18), 2501-2505. https://doi.org/10.1016/S0960-894X%2802%2900508-5

• Journal Article Type: Article
• Acceptance Date: Jul 4, 2002
• Online Publication Date: Aug 15, 2002
• Publication Date: Sep 16, 2002
• Deposit Date: May 12, 2023
• Journal: Bioorganic and Medicinal Chemistry Letters
• Print ISSN: 0960-894X
• Publisher: Elsevier
• Peer Reviewed: Peer Reviewed
• Volume: 12
• Issue: 18
• Pages: 2501-2505
• DOI: https://doi.org/10.1016/S0960-894X%2802%2900508-5
• Public URL: https://nottingham-repository.worktribe.com/output/3137780
• Publisher URL: https://www.sciencedirect.com/science/article/pii/S0960894X02005085?via%3Dihub