Binding affinities of sanggenon derivatives as PTP1B inhibitors; using molecular dynamics and free energy calculations

Kocakaya, Şafak Özhan2024-03-182024-03-182023Kocakaya, Ş. Ö. (2023). Binding affinities of sanggenon derivatives as PTP1B inhibitors; using molecular dynamics and free energy calculations. Azerbaijan Chemical Journal, 2023(4), 71-83.0005-2531https://akj.az/uploads/documents/SOzhanK.pdfhttps://hdl.handle.net/11468/13601Recently, protein tyrosine phosphatase 1B (PTP1B) inhibitors have become the frontier as possible target-ing for anti-cancer and antidiabetic drugs. The contemporary observe represents a pc assisted version to in-vestigate the importance of precise residues within the binding web site of PTP1B with numerous Sang-genon derivatives remoted from nature. Molecular dynamics (MD) simulations were performed to estimate the dynamics of the complexes, and absolute binding unfastened energies have been calculated with exclu-sive additives, and carried out through the usage of the Molecular Mechanics-Poisson-Boltzmann floor re-gion (MM-PB/SA) and Generalized Born surface vicinity (MM-GB/SA) strategies. The effects show that the expected free energies of the complexes are normally constant with the available experimental statis-tics. MM/GBSA free energy decomposition analysis shows that the residues Asp29, Arg24, Met258, and, Arg254 in the second active site in PTP1B are crucial for the excessive selectivity of the inhibitors.eninfo:eu-repo/semantics/closedAccessMM-PBSA analysisMolecular docking Binding energy analysisMolecular dynamics simulationPTP1B inhibitorsSanggenonBinding affinities of sanggenon derivatives as PTP1B inhibitors; using molecular dynamics and free energy calculationsBinding affinities of sanggenon derivatives as PTP1B inhibitors; using molecular dynamics and free energy calculationsArticle2023471832-s2.0-8517691284410.32737/0005-2531-2023-4-71-83Q4