ArticleJournal of molecular recognition : JMR2026
Therapeutic Perspectives of SIRT6 Regulation: Computational Analysis of Activation and Inhibition by Bioactive Molecules.
Article in Journal of molecular recognition : JMR, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Therapeutic Perspectives of SIRT6 Regulation: Computational Analysis of Activation and Inhibition by Bioactive Molecules.Journal of molecular recognition : JMR · 2026Article
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Authors and funding
6 authors.
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Abstract
Sirtuin 6 (SIRT6) is an enzyme belonging to the class of nicotinamide adenine dinucleotide (NAD+) dependent histone deacetylases. It has been of interest due to its multivariate biological role and association with aging-related diseases and metabolic dysfunctions. SIRT6 activation protects against metabolic diseases and aging, and its inhibition is considered a therapy against cancer and inflammation. Here, we explore the modulation of SIRT6 by bioactive molecules, providing a detailed view of the molecular interactions that lead to the activation or inhibition of this protein. Therefore, we investigated the interactions between the ligands quercetin (QUE), isoquercetin (ISO), catechin gallate (CG), and trichostatin A (TSA) with SIRT6, using computational methods from the perspective of molecular modeling through the Molecular Fractionation with Caps Conjugates (MFCC) technique and according to the calculation parameters of Density Functional Theory (DFT). The results revealed the energetic values of each amino acid residue constituting the interaction pocket with the analyzed ligands within a radius of up to 10.0 Å. The analysis of the interaction energies showed an order of priority among the ligands, highlighting CG as the most promising. The observation of the interactions between amino acid residues and ligands identified significant contributions from residues VAL70, PHE64, PHE82, and PHE86. In addition, residues such as PRO62, MET136, MET157, and VAL115 stand out as key components of the protein active site. These findings offer strategic insights into the molecular mechanisms underlying the binding of the studied ligands to SIRT6, providing a deep understanding of their affinity and pharmacological potential.
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Registered trials
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