Conformational entropy and specific affinity of M-cholinolytics and ligands of µ-opioid and D2-dopamine receptors

Abstract

AbstractThe computation model for evaluation of conformational entropy changes upon binding ligands to receptors is described. Then, changes of conformational entropy component and of binding free energy are compared. Interest to conformational entropy arises from developing new drugs as it might be changed purposefully. It is shown that conformational entropy may be used for prediction of affinity to a certain receptor. Examples of directed affinity change under the modification of substances’ conformational flexibility are given. The specific role of the conformational entropy in the receptor’s protection from the irreversible inactivation is identified.