Key Laboratory of Natural Resources of Changbai Mountain & Functional Molecules, Ministry of Education, Yanbian University College of Pharmacy , Yanji , China.
J Enzyme Inhib Med Chem. 2013 Dec;28(6):1199-204. doi: 10.3109/14756366.2012.723206. Epub 2012 Sep 26.
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 4k 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 that 4k was membrane-permeable and enhanced insulin receptor tyrosine phosphorylation in CHO/hIR cells.
一系列 5,7-二羟基黄烷酮衍生物被合成并鉴定为可逆和竞争性蛋白酪氨酸磷酸酶（PTP）1B 抑制剂，其 IC50 值在微摩尔范围内。化合物 4k 对 PTP1B 的体外抑制活性最强（IC50=2.37±0.37μM），对 T 细胞蛋白酪氨酸磷酸酶的选择性最高（3.7 倍）。基于细胞的研究表明，4k 具有膜透过性，并增强 CHO/hIR 细胞中胰岛素受体酪氨酸磷酸化。
