Structural Mechanisms Driving the Selective Efficacy of Oxamniquine against Schistosoma mansoni and Schistosoma japonicum.

ABSTRACT: Oxamniquine (OXA) exhibits selective efficacy against different Schistosoma species, with the highest activity observed in Schistosoma mansoni sulfotransferase (SmSULT) and the lowest in Schistosoma japonicum sulfotransferase (SjSULT). This study utilises advanced atomistic and molecular simulations to elucidate the structural dynamics induced by OXA binding to SmSULT and SjSULT, aiming to unravel the underpinnings of this selective efficacy. Binding free energy (BFE) analyses revealed a markedly higher affinity of OXA for SmSULT (-48.04 kcal/mol) compared to wtSjSULT (-22.84 kcal/mol), with a significant restoration of binding affinity (-39.23 kcal/mol) observed in SjSULT following the mutation of Val139 to Gly139. Comprehensive conformational assessments highlighted that SmSULT-OXA achie

SUBMITTER: Paul-Odeniran KF 

PROVIDER: S-EPMC12414012 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature