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

引用

BIOCELL 2021年第3期45卷 751-759页

作者： SAUD BAWAZER ASGHAR KHAN ABDUR RAUF TAIBI B EN HADDA YAHYA SAL-AWTHAN OMAR BAHATTAB UMER RASHID INAMULLAH KHAN MUHAMMAD A SIF NAWAZ MD SAHAB UDDIN OLATUNDE AHMED MOHAMMAD A LI SHARIATI Department of Pharmaceutical Chemistry Faculty of PharmacyUmm Al-Qura UniversityMakkah21955Saudi Arabia Department of Medicine Khyber Teaching Hospital Peshawar25000Pakistan Department of Chemistry University of SwabiSwabi23430Pakistan LCM Laboratory Mohammed First UniversityFaculty of SciencesOujda60000Morocco Biology Department Faculty of SciencesUniversity of TabukTabuk1144Saudi Arabia Department of Biology Faculty of ScienceIbb UniversityIbbYemen Department of Chemistry COMSATS University IslamabadAbbottabad CampusAbbottabad22060Pakistan Department of Pharmacy University of PeshawarPeshawar25120Pakistan Department of Biotechnology Shaheed Benazir Bhutto UniversitySheringal14400Pakistan Department of Pharmacy Southeast UniversityDhaka1213Bangladesh Pharmakon Neuroscience Research Network Dhaka1207Bangladesh Department of Biochemistry Abubakar Tafawa Balewa UniversityBauchi740272Nigeria Moscow State University of Technologies and Management(The First Cossack University) Moscow119991Russian Federation

Proteintyrosine phosphatase 1B(PTP1B)inhibitionis consideredas a potentialtherapeuticfor the treatmentof cancer,type2 diabetes,*** presentwork,weinvestigatedtheanti-diabeticpotentialof8-hydroxydiospyrin(8-HDN)from *** against the PTP1B *** showed significant inhibitory activity of PTP1B with an IC 50 value of 18.37±0.02μM.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 *** energy data showed that compound 8-HDN is more selective for the allosteric site and hence avoids the problems associated with catalytic site *** inhibition mechanism of 8-HDN can be further investigated as an active lead compound against PTP1B by using in vitro and in vivo models.

关键词： Diospyros lotus Roots 8-hydroxydiospyrin Molecular docking Protein tyrosine phosphatase 1B

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