@Article{biocell.2021.014004,
AUTHOR = {SAUD BAWAZER, ASGHAR KHAN, ABDUR RAUF, TAIBI BEN HADDA, YAHYA S. AL-AWTHAN, OMAR BAHATTAB, UMER RASHID, INAMULLAH KHAN, MUHAMMAD ASIF NAWAZ, MD SAHAB UDDIN, OLATUNDE AHMED, MOHAMMAD ALI SHARIATI},
TITLE = {POM analysis and computational interactions of 8-hydroxydiospyrin inside active site of protein tyrosine phosphatase 1B},
JOURNAL = {BIOCELL},
VOLUME = {45},
YEAR = {2021},
NUMBER = {3},
PAGES = {751--759},
URL = {http://www.techscience.com/biocell/v45n3/41700},
ISSN = {1667-5746},
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 <i>D. lotus</i> against the PTP1B enzyme. It showed significant inhibitory activity of PTP1B with an IC<sub>50</sub> 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 <i>in vitro</i> and <i>in vivo</i> models.},
DOI = {10.32604/biocell.2021.014004}
}