Arylamide derivatives as peptidomimetic inhibitors of calmodulin

Hang Yin, Kendra K. Frederick, Dahui Liu, A. Joshua Wand, William F. DeGrado

Research output: Contribution to journalArticlepeer-review

36 Scopus citations


Many peptides bind to calmodulin (CaM) in a helical conformation. Here we describe a group of synthetic inhibitors of CaM based on an arylamide scaffold that is intended to mimic smMLCK, a CaM-binding helical peptide. Compound 1 showed a K i value of 7.10 ± 1.48 nM in a fluorescence polarization assay that monitors the strong association of CaM and its peptide ligand mastoparan X. ( 1H, 15N)-HSQC NMR spectroscopy experiments suggested that 1 binds to CaM in an analogous fashion to that of smMLCK.

Original languageEnglish (US)
Pages (from-to)223-225
Number of pages3
JournalOrganic Letters
Issue number2
StatePublished - Jan 19 2006

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry


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