MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.--I. Isolation, structural determination and biological properties of MS-271

Bioorg Med Chem. 1996 Jan;4(1):115-20. doi: 10.1016/0968-0896(95)00175-1.

Abstract

A novel cyclic peptide, MS-271, was isolated from the culture broth of an actinomycete, Streptomyces sp. M-271 as an inhibitor of smooth muscle myosin light chain kinase (MLCK). MS-271 inhibited the MLCK from chicken gizzard with an IC50 value of 8 microM. MS-271 did not inhibit cyclic AMP-dependent protein kinase, protein kinase C or calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase at concentrations up to 400 microM. The primary structure of MS-271 was identical to that of siamycin I, an anti-HIV peptide isolated from a microbial source.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Anti-Bacterial Agents
  • Antifungal Agents
  • Cattle
  • Chickens
  • Cyclic AMP-Dependent Protein Kinases / antagonists & inhibitors
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / isolation & purification
  • Enzyme Inhibitors / pharmacology*
  • Fermentation
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Myosin-Light-Chain Kinase / antagonists & inhibitors*
  • Peptides, Cyclic / biosynthesis
  • Peptides, Cyclic / chemistry*
  • Peptides, Cyclic / isolation & purification
  • Peptides, Cyclic / pharmacology*
  • Rats
  • Streptomyces / chemistry*
  • Streptomyces / metabolism

Substances

  • Amino Acids
  • Anti-Bacterial Agents
  • Antifungal Agents
  • Enzyme Inhibitors
  • MS 271
  • Peptides, Cyclic
  • Adenosine Triphosphate
  • Cyclic AMP-Dependent Protein Kinases
  • Myosin-Light-Chain Kinase