All submissions of the EM system will be redirected to Online Manuscript Submission System. Authors are requested to submit articles directly to Online Manuscript Submission System of respective journal.


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

Author(s): S. Bawazeer, A. Rauf1, A. Shahidullah2, A. P. Mishra3*, I. Faraone4,5*, L. Milella4,5, K. Ullah6, G. Uddin7, I. Khan2, S. Patel8 And Z. A. Shah9
Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Umm Al-Qura University, Makkah, P.O. Box 42, Saudi Arabia, 1Department of Chemistry, University of Swabi, Anbar-23561, Khyber Pakhtunkhwa, 2Department of Pharmacy, University of Peshawar, Peshawar-25120, K.P.K, Pakistan, 3Department of Pharmaceutical Chemistry, H. N. B. Garhwal University, Srinagar, Garhwal-246 174, India, 4Department of Science, 5Spinoff BioActiPlant s.r.l., University of Basilicata, V.le dell'Ateneo Lucano, 10, 85100 Potenza, Italy, 6Department of Zoology, University of Swabi, Anbar-23561, Khyber Pakhtunkhwa, 7Institute of Chemical Sciences, University of Peshawar, Peshawar-25120, K.P.K, Pakistan, 8Bioinformatics and Medical Informatics Research Center, San Diego State University, San Diego-92182, USA, 9Department of Chemistry, The University of Agriculture Peshawar, Peshawar-25120, Pakistan

Correspondence Address:
Department of Pharmaceutical Chemistry, H. N. B. Garhwal University, Srinagar Garhwal-246 174, India, E-mail:

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.

Full-Text | PDF

Google scholar citation report
Citations : 66710

Indian Journal of Pharmaceutical Sciences received 66710 citations as per google scholar report