Peptide truncation leads to a twist and an unusual increase in affinity for casitas B-lineage lymphoma tyrosine kinase binding domain

Eric A. Kumar, Ziyan Yuan, Nicholas Y. Palermo, Lin Dong, Gulzar Ahmad, G. L. Lokesh, Carol Kolar, Smitha Kizhake, Gloria E Borgstahl, Hamid Band, Amarnath Natarajan

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

We describe truncation and SAR studies to identify a pentapeptide that binds Cbl tyrosine kinase binding domain with a higher affinity than the parental peptide. The pentapeptide has an alternative binding mode that allows occupancy of a previously uncharacterized groove. A peptide library was used to map the binding site and define the interface landscape. Our results suggest that the pentapeptide is an ideal starting point for the development of inhibitors against Cbl driven diseases.

Original languageEnglish (US)
Pages (from-to)3583-3587
Number of pages5
JournalJournal of Medicinal Chemistry
Volume55
Issue number7
DOIs
StatePublished - Apr 12 2012

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

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