Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA, USA.
FEBS J. 2010 May;277(9):2096-108. doi: 10.1111/j.1742-4658.2010.07623.x. Epub 2010 Mar 22.
The protein arginine methyltransferase (PRMT) family of enzymes catalyzes the transfer of methyl groups from S-adenosylmethionine to the guanidino nitrogen atom of peptidylarginine to form monomethylarginine or dimethylarginine. We created several less polar analogs of the specific PRMT inhibitor arginine methylation inhibitor-1, and one such compound was found to have improved PRMT inhibitory activity over the parent molecule. The newly identified PRMT inhibitor modulated T-helper-cell function and thus may serve as a lead for further inhibitors useful for the treatment of immune-mediated disease.
蛋白质精氨酸甲基转移酶（PRMT）家族的酶催化 S-腺苷甲硫氨酸的甲基从胍基氮原子转移到肽基精氨酸，形成单甲基精氨酸或二甲基精氨酸。我们创建了几种特定的 PRMT 抑制剂精氨酸甲基化抑制剂-1 的极性较小的类似物，其中一种化合物被发现比母体分子具有更好的 PRMT 抑制活性。新鉴定的 PRMT 抑制剂调节 T 辅助细胞功能，因此可能成为进一步用于治疗免疫介导疾病的抑制剂的先导。
