Isolation and characterization of N98-1272 A, B and C, selective acetylcholinesterase inhibitors from metabolites of an actinomycete strain

J Enzyme Inhib Med Chem. 2007 Feb;22(1):43-9. doi: 10.1080/14756360600988781.

Abstract

A high throughput screening was carried out in order to search for inhibitors of acetylcholinesterase (AChE) from microorganism metabolites. An actinomycete strain was found to produce active compounds named N98-1272 A, B and C with IC50 of 15.0, 11.5, 12.5 microM, respectively. Structural studies revealed that the three compounds are identical to the known antibiotics, Manumycin C, B and A. Kinetic analyses showed that N98-1272 C (Manumycin A) acted as a reversible noncompetitive inhibitor of acetylcholinesterase, with a Ki value of 7.2 microM. The cyclohexenone epoxide part of the structure plays a crucial role in the inhibitory activity against AChE. Compared with Tacrine, N98-1272 A, B, and C exhibit much better selectivity toward AChE over BuChE.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / drug effects*
  • Actinobacteria / chemistry*
  • Cholinesterase Inhibitors / isolation & purification*
  • Cholinesterase Inhibitors / pharmacology*
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Spectrometry, Mass, Fast Atom Bombardment
  • Structure-Activity Relationship

Substances

  • Cholinesterase Inhibitors
  • Acetylcholinesterase