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Effect of β-cyclodextrin-EGCG complexion against aggregated a-synuclein through density functional theory and discrete molecular dynamics
Srinivasan E,
Published in Elsevier BV
Volume: 717
Pages: 38 - 46
Misfolding and aggregation of a-synuclein (AS) protein are considered to be causative factors for Parkinson's disease. Herein, we describe molecular dynamics simulations of aggregated AS with βC-EGCG to better characterize the detailed conformational effects on their inhibitory action. Our results indicate that the binding of βC-EGCG disrupt the β-sheet of aggregated AS structure and cause impairment of intermolecular interactions. Furthermore, the free energy landscape portrayed the effect of βC-EGCG directly impedes the formation of aggregated intermediate conformers in AS. Hence, our study could aid in the field of structure-based drug design against the AS disorder. © 2019 Elsevier B.V.
About the journal
JournalData powered by TypesetChemical Physics Letters
PublisherData powered by TypesetElsevier BV
Open AccessNo