Quantum chemical and molecular mechanics studies on the assessment of interactions between resveratrol and mutant SOD1 (G93A) protein.

摘要: Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease that has been associated with mutations in metalloenzyme superoxide dismutase (SOD1) causing protein structural destabilization and aggregation. However, the mechanistic action cure for still remain obscure. Herein, we initially studied conformational preferences of SOD1 structures upon substitution Ala at Gly93 comparison wild type. Our results corroborated previous experimental studies on aggregation destabilizing activity mutant G93A. On therapeutic point view, computationally analyzed influence resveratrol, natural polyphenol widely found red wine relative to type, using molecular docking studies. Further, FMO calculations were performed, GAMESS study pair residual interaction type complex systems. Consequently, resveratrol showed greater than Subsequently, evaluated systems, where earlier lose their stability was regained, binding resveratrol. Similar trend 2-D free energy landscapes both Hence, combined biophysical quantum chemical our supported studies, thereby stipulating an paving way design highly potent effective inhibitors against fALS affecting mankind.