Isolation of Acetylcholinesterase Inhibiting Peptides from Conus mustelinus venom

Abstract

Venom from Conus is known to contain peptides which inhibit the function of ion channels and neurotransmitter receptors, but an effort to evaluate its inhibition against acetylcholinesterase (AchE) has yet to be conducted. Through El Iman's colorimetric method and Mus musculus bioassay, the crude venom extract and purified peptide venom fractions from Conus mustelinus were investigated for in vivo and in vitro AchE inhibition activities. The crude extract was found to have significant AchE inliibitory activity (28.9% in vivo and 54.1% in vitro) and of the two peptide fractions isolated, Potential AchE Inhibiting Fraction-10(PAIF-l 0, eluted at 21.15% B90) was also found to significantly inhibit AchE (30.5% in vivo and 44.8% in vitro), however no significant activity against AchE was observed from PAIF-11 (eluted at 20.68% B90) which inhibited it by 8.9% in vivo and -4.9% in vitro. Inhibition of AchE activity by Conus venom thus provides a promising approach to drug formulation.