Skeletal, smooth and cardiac muscle myosin 2 are less sensitive for the chiral hydroxyl moiety of blebbistatin than that of non-muscle myosin 2 isoforms

Abstract

Myosin 2 inhibition and the traditional myosin 2 inhibitor, blebbistatin have recently become the focus of interest of drug discovery and drug development. The effect of several substitutions on myosin inhibitory properties and other properties like solubility or photostability have already been characterized, however, some basic ideas related to the structure have not been experimentally confirmed yet. Since its discovery blebbistatin's chiral hydroxyl moiety has been accepted as a crucial determinant of the inhibitory efficiency.