POM analysis and computational interactions of 8-hydroxydiospyrin inside active site of protein tyrosine phosphatase 1B

[摘要] Protein tyrosine phosphatase 1B (PTP1B) inhibition is considered as a potential therapeutic for the treatment of cancer, type 2 diabetes, and obesity. In our present work, we investigated the anti-diabetic potential of 8-hydroxydiospyrin (8-HDN) from D. lotus against the PTP1B enzyme. It showed significant inhibitory activity of PTP1B with an IC 50 value of 18.37 ± 0.02 μM. A detailed molecular docking study was carried out to analyze the binding orientation, binding energy, and mechanism of inhibition. A comparative investigation of 8-HDN in the catalytic, as well as the allosteric site of PTP1B, was performed. Binding energy data showed that compound 8-HDN is more selective for the allosteric site and hence avoids the problems associated with catalytic site inhibition. The inhibition mechanism of 8-HDN can be further investigated as an active lead compound against PTP1B by using in vitro and in vivo models.

[学科分类] 仪器

[关键词] Diospyros lotus;Roots;8-Hydroxydiospyrin;Molecular docking;Protein tyrosine phosphatase 1B