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

J Cell Biochem. 1985;29(2):83-93. doi: 10.1002/jcb.240290204.


Based on a consideration of the probable structure of calmodulin and some 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 dissociation constants for binding (less than or equal to 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Brain / metabolism
  • Calmodulin / antagonists & inhibitors*
  • Calmodulin-Binding Proteins / chemical synthesis*
  • Circular Dichroism
  • Kinetics
  • Protein Binding
  • Protein Conformation
  • Spectrometry, Fluorescence
  • Structure-Activity Relationship


  • Calmodulin
  • Calmodulin-Binding Proteins