4.2 Article

Structural Insights Behind Protein Tyrosine Phosphatase 1B Inhibitory Activity of Diospyrin

Journal

INDIAN JOURNAL OF PHARMACEUTICAL SCIENCES
Volume 81, Issue 3, Pages 565-568

Publisher

INDIAN PHARMACEUTICAL ASSOC
DOI: 10.36468/pharmaceutical-sciences.546

Keywords

Diospyros lotus; Ebenaceae; diospyrin; PTP1B; molecular docking

Funding

  1. Higher Education Commission

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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 mu M). 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.

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