Tully David C, Liu Hong, Alper Phil B, Chatterjee Arnab K, Epple Robert, Roberts Michael J, Williams Jennifer A, Nguyen KhanhLinh T, Woodmansee David H, Tumanut Christine, Li Jun, Spraggon Glen, Chang Jonathan, Tuntland Tove, Harris Jennifer L, Karanewsky Donald S
Genomics Institute of the Novartis Research Foundation, 10675 John J. Hopkins Dr., San Diego, CA 92121, USA.
Bioorg Med Chem Lett. 2006 Apr 1;16(7):1975-80. doi: 10.1016/j.bmcl.2005.12.095. Epub 2006 Jan 30.
A series of N(alpha)-2-benzoxazolyl-alpha-amino acid-(arylaminoethyl)amides were identified as potent, selective, and noncovalent inhibitors of cathepsin S. Structure-activity relationships including strategies for modulating the selectivities among cathepsins S, K, and L, and in vivo pharmacokinetics are discussed. A X-ray structure of compound 3 bound to the active site of cathepsin S is also reported.
一系列N（α）-2-苯并恶唑基-α-氨基酸-（芳基氨基乙基）酰胺被鉴定为组织蛋白酶S的强效、选择性和非共价抑制剂。讨论了构效关系，包括调节组织蛋白酶S、K和L之间选择性的策略以及体内药代动力学。还报道了化合物3与组织蛋白酶S活性位点结合的X射线结构。
