Interaction of Cyclic Peptides and Depsipeptides with Calmodulin

Abstract

A variety of small peptides including hormones, neurotransmitters, and insect venom components such as ACTH, Beta endorphin, and melittin, respectively, bind calmodulin (CaM) and inhibit CaM-dependent enzyme activity. The binding has been shown to be of high affinity; saturable; calcium dependent; and, upon the removal of calcium, reversible. Peptides bind CaM in either a 1:1 or 1:2 molar ratio and can be competitively displaced from CaM by other non- peptide CaM antagonists such as phenothiazines. Structure-activity studies have demonstrated that most CaM-binding peptides possess either basic amino acids, hydrophobic amino acids, or alpha helical secondary structure.

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Document Details

Document Type
Technical Report
Publication Date
Apr 10, 1990
Accession Number
ADA221278

Entities

People

  • A. B. Fajer
  • K. A. Mereish
  • R. Solow

Organizations

  • United States Army Medical Research Institute of Infectious Diseases

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Abstracts
  • Acids
  • Amino Acids
  • Basic Amino Acids
  • Biomedical Research
  • Classification
  • Emission Spectra
  • Enzymes
  • Fluorescence
  • Hydrophobic Properties
  • Inhibition
  • Intensity
  • Molybdic Acids
  • Nucleotides
  • Quantum Yields
  • Quenching
  • Security

Fields of Study

  • Chemistry

Readers

  • Molecular and Cellular Biochemistry