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dc.contributor.authorNitchakan Daraien_US
dc.contributor.authorPanupong Mahalapbutren_US
dc.contributor.authorKanyani Sangpheaken_US
dc.contributor.authorChompoonut Rungnimen_US
dc.contributor.authorPeter Wolschannen_US
dc.contributor.authorNawee Kungwanen_US
dc.contributor.authorThanyada Rungrotmongkolen_US
dc.description.abstract© 2020, Prince of Songkla University. All rights reserved. The Epstein-Barr nuclear antigen 1 (EBNA1) is a crucial protein expressed by the Epstein-Barr virus (EBV). The EBNA1 is necessary for the replication and transcriptional regulation of latent gene expression of the EBV. Therefore, it is connected with some diseases, especially malignancies. Previous studies have shown that chalcone potentially inhibited the EBV virus; therefore, in this study a series of chalcones were screened in silico toward EBNA1 by the use molecular docking and molecular dynamics simulation. The results suggested that chalcone 3a displayed significantly greater binding affinity than the reported anti-EBV agents. The EBNA1 residues K477, I481, N519, K586, and T590 contributed mainly for the chalcone 3a binding at the recognition helix site. Altogether, this chalcone might serve as a lead compound acting against EBNA1.en_US
dc.titleIn silico screening of chalcones against epstein-barr virus nuclear antigen 1 proteinen_US
article.title.sourcetitleSongklanakarin Journal of Science and Technologyen_US
article.volume42en_US Universityen_US Wienen_US National Nanotechnology Centeren_US Mai Universityen_US
Appears in Collections:CMUL: Journal Articles

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