Poster Presentations

Start Date

20-5-2014 12:30 PM

Description

Many biologically active polyphenols have been recognized for their beneficial effects in managing diabetes and their complications. However, the mechanisms behind their functions are poorly understood. As protein-tyrosine phosphatase 1B (PTP1B) has been identified as a target for anti-diabetic agents, the potential inhibitory effects of a dozen structurally diverse polyphenol natural products have been investigated. Among these polyphenols, potent inhibitory activities have been identified for 6 of them with IC50 in micromolar range, while the other polyphenols showed very weak inhibition. A structure-activity relationship (SAR) study and molecular ducking results suggest that both a rigid planar 3-ring backbone and appropriate substitutions of hydroxyl groups benefit the inhibitory activity. The mechanism of inhibition of PTP1B was further investigated by Michaelis-Menten kinetics and the inhibition mode for PTP1B was determined along with the inhibition constant.

Comments

Abstract of poster presented at the 2014 UMass Center for Clinical and Translational Science Research Retreat, held on May 20, 2014 at the University of Massachusetts Medical School, Worcester, Mass.

Creative Commons License

Creative Commons Attribution-Noncommercial-Share Alike 3.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-Share Alike 3.0 License.

Share

COinS
 
May 20th, 12:30 PM

Inhibition of Protein Tyrosine Phosphatase 1B by Polyphenol Natural Products: Relevant to Diabetes Management

Many biologically active polyphenols have been recognized for their beneficial effects in managing diabetes and their complications. However, the mechanisms behind their functions are poorly understood. As protein-tyrosine phosphatase 1B (PTP1B) has been identified as a target for anti-diabetic agents, the potential inhibitory effects of a dozen structurally diverse polyphenol natural products have been investigated. Among these polyphenols, potent inhibitory activities have been identified for 6 of them with IC50 in micromolar range, while the other polyphenols showed very weak inhibition. A structure-activity relationship (SAR) study and molecular ducking results suggest that both a rigid planar 3-ring backbone and appropriate substitutions of hydroxyl groups benefit the inhibitory activity. The mechanism of inhibition of PTP1B was further investigated by Michaelis-Menten kinetics and the inhibition mode for PTP1B was determined along with the inhibition constant.

 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.