Synthesis and characterization of 5, 7-dihydroxyflavanone derivatives as novel protein tyrosine phosphatase 1B inhibitors. (December 2013)

• Record Type: Journal Article
• Authors: Sun, Liang-Peng; Ma, Wei-Ping; Gao, Li-Xin; Yang, Ling-Ling; Quan, Ying-Chun; Li, Jia; Piao, Hu-Ri
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 28:Number 6(2013:Dec.)
• Page Start: 1199
• Page End: 1204
• Publication Date: 2013-12
• Subjects: Protein tyrosine phosphatase 1B -- inhibitors -- 5, 7-dihydroxyflavanone -- structure–activity relationship -- diabetes; Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.3109/14756366.2012.723206
• Languages: English
• ISSNs: 1475-6366

Abstract

Abstract : A series of 5, 7-dihydroxyflavanone derivatives were synthesized and identified as reversible and competitive protein tyrosine phosphatase (PTP) 1B inhibitors with IC50 values in the micromolar range. Compound4k had the most potent in vitro inhibition activity against PTP1B (IC50 = 2.37 ± 0.37 μM) and the greatest selectivity (3.7-fold) for PTP1B relative to T-cell protein tyrosine phosphatase. Cell-based studies revealed that4k was membrane-permeable and enhanced insulin receptor tyrosine phosphorylation in CHO/ h IR cells.