化学
NS5B
变构调节
药物发现
进入抑制剂
药理学
生物化学
病毒学
肝炎病毒
病毒复制
病毒进入
病毒
受体
生物
基因
基因型
作者
Kap‐Sun Yeung,Brett R. Beno,Kyle Parcella,John A. Bender,Katherine A. Grant-Young,Andrew Nickel,Prashantha Gunaga,Prakash Anjanappa,Rajesh O. Bora,K. Selvakumar,Karen Rigat,Ying-Kai Wang,Mengping Liu,Julie A. Lemm,Kathy Mosure,S. Sheriff,Changhong Wan,Mark R. Witmer,Kevin Kish,Umesh Hanumegowda
标识
DOI:10.1021/acs.jmedchem.7b00328
摘要
The hepatitis C virus (HCV) NS5B replicase is a prime target for the development of direct-acting antiviral drugs for the treatment of chronic HCV infection. Inspired by the overlay of bound structures of three structurally distinct NS5B palm site allosteric inhibitors, the high-throughput screening hit anthranilic acid 4, the known benzofuran analogue 5, and the benzothiadiazine derivative 6, an optimization process utilizing the simple benzofuran template 7 as a starting point for a fragment growing approach was pursued. A delicate balance of molecular properties achieved via disciplined lipophilicity changes was essential to achieve both high affinity binding and a stringent targeted absorption, distribution, metabolism, and excretion profile. These efforts led to the discovery of BMS-929075 (37), which maintained ligand efficiency relative to early leads, demonstrated efficacy in a triple combination regimen in HCV replicon cells, and exhibited consistently high oral bioavailability and pharmacokinetic parameters across preclinical animal species. The human PK properties from the Phase I clinical studies of 37 were better than anticipated and suggest promising potential for QD administration.
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