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dc.contributor.authorLiu, Zhiwei
dc.contributor.authorGuo, Maolin
dc.date2022-08-11T08:08:14.000
dc.date.accessioned2022-08-23T15:47:33Z
dc.date.available2022-08-23T15:47:33Z
dc.date.issued2014-05-20
dc.date.submitted2014-10-10
dc.identifier.doi10.13028/drhm-q743
dc.identifier.urihttp://hdl.handle.net/20.500.14038/28011
dc.description<p>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.</p>
dc.description.abstractMany 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.
dc.formatyoutube
dc.language.isoen_US
dc.rightsCopyright the Author(s)
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/
dc.subjectBiochemistry
dc.subjectNutritional and Metabolic Diseases
dc.subjectOrganic Chemicals
dc.subjectTranslational Medical Research
dc.titleInhibition of Protein Tyrosine Phosphatase 1B by Polyphenol Natural Products: Relevant to Diabetes Management
dc.typePoster Abstract
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1313&amp;context=cts_retreat&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cts_retreat/2014/posters/93
dc.identifier.contextkey6226177
refterms.dateFOA2022-08-23T15:47:33Z
html.description.abstract<p>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.</p>
dc.identifier.submissionpathcts_retreat/2014/posters/93


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