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: Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.3109/14756366.2012.723206
• Languages: English
• ISSNs: 1475-6366

Abstract

<abstract> <title> <x xml:space="preserve">Abstract</x> </title> <p>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. Compound <bold>4k</bold> had the most potent <italic>in vitro</italic> 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 that <bold>4k</bold> was membrane-permeable and enhanced insulin receptor tyrosine phosphorylation in CHO/<italic>h</italic>IR cells.</p> </abstract>