In Silico Binding Affinities of the Molecules in Camellia Sinensis Teas to NLRP3 NACHT Domain
Abstract
NLRP3 inflammasome secretes proinflammatory cytokines in response to microbial infection and cellular damage, induces pyroptotic cell death, and triggers many pathological conditions. For this reason, it is important to determine the products that can inhibit the NLRP3 protein. In this study, the affinities of 27 molecules in Camellia sinensis tea species to ADP and inhibitor cavities in the NACHT domain of NLRP3 were analyzed in silico using molecular docking, molecular dynamics simulation, and free energy calculation method MM/GBSA. Among the components, theaflavic acid, (-)-epicatechin gallate and (-)-epigallocatechin gallate gave better binding affinities. It was concluded that it would be beneficial to conduct advanced studies on whether these three compounds contribute to the preventability of NLRP3-mediated inflammatory diseases.
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