Miller Rand M, Taunton Jack
Chemistry and Chemical Biology Graduate Program, University of California, San Francisco, California, USA.
Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California, USA.
Methods Enzymol. 2014;548:93-116. doi: 10.1016/B978-0-12-397918-6.00004-5.
Protein kinase inhibitors are an important class of therapeutics. In addition, selective kinase inhibitors can often reveal unexpected biological insights, augmenting genetic approaches and playing a decisive role in preclinical target validation studies. Nevertheless, developing protein kinase inhibitors with sufficient selectivity and pharmacodynamic potency presents significant challenges. Targeting noncatalytic cysteines with covalent inhibitors is a powerful approach to address both challenges simultaneously. Here, we describe our efforts to design irreversible and reversible electrophilic inhibitors with varying degrees of kinase selectivity. Highly selective covalent inhibitors have been used to elucidate the roles of p90 ribosomal protein S6 kinases in animal models of atherosclerosis and diabetes. By contrast, semipromiscuous covalent inhibitors have revealed new therapeutic targets in disease-causing parasites and have shown utility as chemoproteomic probes for interrogating kinase occupancy in living cells.
蛋白激酶抑制剂是一类重要的治疗药物。此外,选择性激酶抑制剂常常能揭示出意想不到的生物学见解,增强基因研究方法,并在临床前靶点验证研究中发挥决定性作用。然而,开发具有足够选择性和药效学效力的蛋白激酶抑制剂面临重大挑战。用共价抑制剂靶向非催化性半胱氨酸是同时应对这两个挑战的有力方法。在此,我们描述了我们设计具有不同程度激酶选择性的不可逆和可逆亲电抑制剂的努力。高选择性共价抑制剂已被用于阐明p90核糖体蛋白S6激酶在动脉粥样硬化和糖尿病动物模型中的作用。相比之下,半混杂共价抑制剂已在致病寄生虫中揭示了新的治疗靶点,并已显示出作为化学蛋白质组学探针用于检测活细胞中激酶占有率的效用。