Development of stapled helical peptides to perturb the Cdt1–Mcm6 interaction‡. (28th April 2015)

• Record Type: Journal Article
• Authors: Lee, Jonghan Peter; Liu, Changdong; Li, Tianlu; Zhu, Guang; Li, Xuechen; Liu, Lei; Xu, Jiaxi
• Is Part Of: Journal of peptide science. Volume 21:Number 7(2015:Jul.)
• Page Start: 593
• Page End: 598
• Publication Date: 2015-04-28
• Subjects: Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.2779
• Languages: English
• ISSNs: 1075-2617

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Six all‐hydrocarbon‐stapled Cdt1 MBD‐derived peptides have been designed and synthesized to perturb the Cdt1–Mcm6 interaction, which is involved in DNA replication. Inconsistency between the helicity of the obtained peptidomimetics and their binding affinity has been observed. The helicity of 13‐amino acid stapled peptides increased, while their binding to Mcm6 was decreased. On the other hand, the 30‐amino acid stapled peptides exhibited decreased helicity but increased binding affinity. Copyright © 2015 European Peptide Society and John Wiley &amp; Sons, Ltd.</p> </abstract>