Structural Insights Behind Protein Tyrosine Phosphatase 1B Inhibitory Activity of Diospyrin
| Autor: | S Bawazeer, A Rauf, A Shahidullah, A. P Mishra, I Faraone, L Milella, K Ullah, G Uddin, I Khan, S Patel, Z. A Shah |
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| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
biology In silico Molecular binding Active site Inhibitory postsynaptic potential 030226 pharmacology & pharmacy Protein Tyrosine Phosphatase 1B 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Enzyme chemistry Biochemistry biology.protein IC50 Lead compound |
| Zdroj: | Indian Journal of Pharmaceutical Sciences. 81 |
| DOI: | 10.36468/pharmaceutical-sciences.546 |
| Popis: | The present study was designed to evaluate the antidiabetic potential of diospyrin isolated from Diospyros lotus, using protein tyrosine phosphatase 1B enzyme as the target. Molecular binding mode of diospyrin to protein tyrosine phosphatase 1B was essential to explore its molecular interactions. Molecular docking, the simulation technique used to model the interaction between two molecules were performed using Open Eye software. This compound exhibited significant protein tyrosine phosphatase 1B inhibitory activity (IC50 value: 27.59±0.03 μM). Molecular docking studies showed significant molecular interactions of the diospyrin with Gly 220, Tyr 46, Val 49 and Asp 48 inside the active site of protein tyrosine phosphatase 1B. The in silico result builds prospect that diospyrin can be further developed as a new lead compound targeting protein tyrosine phosphatase 1B inhibition. |
| Databáze: | OpenAIRE |
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