International Journal of Pharma and Bio Sciences
ijpbs.net
editorijpbs@rediffmail.com (or) editorofijpbs@yahoo.com (or) prasmol@rediffmail.com
10.22376/ijpbs.2019.10.1.p1-12
Volume 3 Issue 4
2012(October - December)
DOCKING OF RHEUM EMODI COMPOUNDS AGAINST PROTEIN TYROSINE PHOSPHATASE 1B
Protein Tyrosine Phosphatase 1B (PTP1B) has been shown to be a negative regulator of insulin signaling by dephosphorylating key tyrosine residues within the regulatory domain of the β-subunit of the insulin receptor. Also PTP1B is involved in the down regulation of insulin and leptin signaling. Design of small molecule compounds inhibiting the enzymatic function of PTP1B is of great medicinal interest. The aim of the study is to design tyrosine kinase inhibitors from the plant lessThan i greaterThan Rheum emodi lessThan /i greaterThan derived compounds namely Emodin and Chrysophanol. These plant derived compounds leads to stronger interaction with PTP1B when compared to the diabetic drug Glibenclamide.
RADHIKA R AND DR SUDARSANAM D
Protein tyrosine phosphatase1B (PTP1B), Auto phosphorylation, Docking, Emodin and Chrysophanol.
1150-1154