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• W4284706384 abstract "Hydroxychloroquine (HCQ) is an important drug that is in the trial stage for different types of cancer diseases; however, insight about the mechanism of its action is almost unknown. G-quadruplex (Gq) has been considered one of the potential targets for the cure of cancer; hence, it is essential to understand the possibility of the binding of HCQ with Gq to get a better understanding of its action. In this study, the molecular insight into the possibility of the binding of HCQ with different topological forms of Gq of the human telomere (htel) has been investigated using spectroscopic, thermochemical, and molecular dynamics simulation techniques. The spectroscopic and thermochemical studies clearly suggest that HCQ has a topological preference in the binding with htel in the form of a hybrid structure rather than the antiparallel form and the binding of HCQ stabilizes preferably to the hybrid form. The molecular dynamics simulation study suggests that the interaction of HCQ in the groove and loop regions of the hybrid structure is more stable compared to the antiparallel form, which is the probable reason for the topological preference of HCQ. This study depicts that HCQ has a topological preference in the binding and stabilization of the Gq of htel, which makes it potentially an important drug for targeting the telomere region associated with cancer disease." @default.
• W4284706384 created "2022-07-08" @default.
• W4284706384 creator A5023702917 @default.
• W4284706384 creator A5036174099 @default.
• W4284706384 creator A5091549782 @default.
• W4284706384 date "2022-07-06" @default.
• W4284706384 modified "2023-09-24" @default.
• W4284706384 title "Spectroscopic and Molecular Dynamics Aspect of Antimalarial Drug Hydroxychloroquine Binding with Human Telomeric G-Quadruplex" @default.
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• W4284706384 doi "https://doi.org/10.1021/acs.jpcb.2c03267" @default.
• W4284706384 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35793709" @default.
• W4284706384 hasPublicationYear "2022" @default.
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