NIH Chemical Genomic Center, National Human Genome Research Institute, National Institutes of Health, 9800 Medical Center Drive, Rockville, Maryland, United States.
J Med Chem. 2011 Feb 24;54(4):1033-58. doi: 10.1021/jm1008902. Epub 2011 Jan 20.
Gaucher disease is a lysosomal storage disorder (LSD) caused by deficiency in the enzyme glucocerebrosidase (GC). Small molecule chaperones of protein folding and translocation have been proposed as a promising therapeutic approach to this LSD. Most small molecule chaperones described in the literature contain an iminosugar scaffold. Here we present the discovery and evaluation of a new series of GC inhibitors with a quinazoline core. We demonstrate that this series can improve the translocation of GC to the lysosome in patient-derived cells. To optimize this chemical series, systematic synthetic modifications were performed and the SAR was evaluated and compared using three different readouts of compound activity: enzymatic inhibition, enzyme thermostabilization, and lysosomal translocation of GC.
戈谢病是一种溶酶体贮积症(LSD),由葡萄糖脑苷脂酶(GC)缺乏引起。蛋白质折叠和易位的小分子伴侣已被提议作为治疗这种 LSD 的一种很有前途的方法。文献中描述的大多数小分子伴侣都含有亚氨基糖支架。在这里,我们展示了一种具有喹唑啉核心的新型 GC 抑制剂系列的发现和评估。我们证明,该系列可以改善患者来源细胞中 GC 向溶酶体的易位。为了优化这个化学系列,我们进行了系统的合成修饰,并使用 GC 的酶抑制、酶热稳定性和溶酶体易位的三种不同的化合物活性读数来评估和比较 SAR。