The design, synthesis, and characterization of tight‐binding inhibitors of calmodulin

William F. DeGrado, Frank G. Prendergast, Henry R. Wolfe, Jos A. Cox

Research output: Contribution to journalArticlepeer-review

47 Scopus citations


Based on a consideration of the probable structure of calmodulin and sonic natural peptides known to interact with it, two calmodulin‐binding peptides were designed. These peptides bind to calmodulin in helical conformations and are capable of forming electrostatic and hydrophobic interactions with calmodulin. Their dissocation constants for binding (⩽ 210 and 400 pM) place them as the tightest‐binding inhibitors of calmodulin thus far reported. The study of the interactions of these and similar peptides with calmodulin will provide valuable insights into the mechanisms whereby calmodulin binds to target enzymes, and it also serves as an excellent model system for exploring the physical chemistry of protein‐protein interaction.

Original languageEnglish (US)
Pages (from-to)83-93
Number of pages11
JournalJournal of cellular biochemistry
Issue number2
StatePublished - 1985


  • calmodulin
  • calmodulin‐peptide interactions
  • peptide design

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'The design, synthesis, and characterization of tight‐binding inhibitors of calmodulin'. Together they form a unique fingerprint.

Cite this