Open Access

ARTICLE

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

SAUD BAWAZER¹, ASGHAR KHAN², ABDUR RAUF^3,*, TAIBI BEN HADDA⁴, YAHYA S. AL-AWTHAN^5,6, OMAR BAHATTAB⁵, UMER RASHID⁷, INAMULLAH KHAN⁸, MUHAMMAD ASIF NAWAZ⁹, MD SAHAB UDDIN^10,11, OLATUNDE AHMED¹², MOHAMMAD ALI SHARIATI¹³

1 Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Umm Al-Qura University, Makkah, 21955, Saudi Arabia
2 Department of Medicine Khyber Teaching Hospital, Peshawar, 25000, Pakistan
3 Department of Chemistry, University of Swabi, Swabi, 23430, Pakistan
4 LCM Laboratory, Mohammed First University, Faculty of Sciences, Oujda, 60000, Morocco
5 Biology Department, Faculty of Sciences, University of Tabuk, Tabuk, 1144, Saudi Arabia
6 Department of Biology, Faculty of Science, Ibb University, Ibb, Yemen
7 Department of Chemistry, COMSATS University Islamabad, Abbottabad Campus, Abbottabad, 22060, Pakistan
8 Department of Pharmacy, University of Peshawar, Peshawar, 25120, Pakistan
9 Department of Biotechnology, Shaheed Benazir Bhutto University, Sheringal, 14400, Pakistan
10 Department of Pharmacy, Southeast University, Dhaka, 1213, Bangladesh
11 Pharmakon Neuroscience Research Network, Dhaka, 1207, Bangladesh
12 Department of Biochemistry, Abubakar Tafawa Balewa University, Bauchi, 740272, Nigeria
13 Moscow State University of Technologies and Management (The First Cossack University), Moscow, 119991, Russian Federation

* Corresponding Author: Abdur Rauf. Email:

BIOCELL 2021, 45(3), 751-759. https://doi.org/10.32604/biocell.2021.014004

Received 28 August 2020; Accepted 27 November 2020; Issue published 03 March 2021

Abstract

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 IC₅₀ 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.

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