Binding affinities of sanggenon derivatives as PTP1B inhibitors; using molecular dynamics and free energy calculations
Yükleniyor...
Tarih
2023
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Azerbaijan National Academy of Sciences
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
Recently, 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.
Açıklama
Anahtar Kelimeler
MM-PBSA analysis, Molecular docking Binding energy analysis, Molecular dynamics simulation, PTP1B inhibitors, Sanggenon
Kaynak
Azerbaijan Chemical Journal
WoS Q Değeri
Scopus Q Değeri
Q4
Cilt
2023
Sayı
4
Künye
Kocakaya, 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.
