Communication
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Unearthing Novel Insights: Hypericin's Interaction with Heat Shock Proteins
Version 1
: Received: 27 November 2023 / Approved: 28 November 2023 / Online: 29 November 2023 (09:58:27 CET)
How to cite: FERRARI, I. V. Unearthing Novel Insights: Hypericin's Interaction with Heat Shock Proteins. Preprints 2023, 2023111840. https://doi.org/10.20944/preprints202311.1840.v1 FERRARI, I. V. Unearthing Novel Insights: Hypericin's Interaction with Heat Shock Proteins. Preprints 2023, 2023111840. https://doi.org/10.20944/preprints202311.1840.v1
Abstract
Heat Shock Proteins play a crucial role in maintaining cellular integrity during thermal stress conditions, acting as chaperones and participating in the regulation of cellular responses. The focus was to contribute valuable insights into the potential role of hypericin in modulating these heat shock proteins and its implications for anti-tumoral properties. This study employs computational methods, specifically molecular docking, to investigate the potential biological interactions between the chaperone proteins HSP90 and HSC70 and Hypericin, a natural compound recognized for its anti-tumor properties. Despite the limited existing studies in this domain, this research aims to uncover structural insights into the binding mechanisms between Hypericin and these heat shock proteins. In the docking assessments, hypericin demonstrated notable binding energy results, exhibiting a binding energy of -10.5 kcal/mol with Heat Shock Cognate 71 kDa protein and -11.2 kcal/mol with Heat Shock Protein HSP90-alpha.
Keywords
HSP90 protein; HSC70 protein; docking study; hypericin
Subject
Public Health and Healthcare, Public Health and Health Services
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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