化学
对接(动物)
亲缘关系
受体
立体化学
组合化学
药物发现
大麻素受体
计算生物学
分子
结合亲和力
小分子
结构-活动关系
蛋白质-配体对接
兴奋剂
分子模型
大麻素受体2型
活动站点
结合位点
生物化学
大麻素
化学合成
药理学
化学图书馆
大麻素受体激动剂
作者
Moira Rachman,Christos Iliopoulos‐Tsoutsouvas,M. Sacco,X X Xu,Cheng-Guo Wu,Emma Santos,Isabella S. Glenn,Lu Paris,Michelle K. Cahill,Suthakar Ganapathy,Tia A. Tummino,Yurii S. Moroz,Dmytro S. Radchenko,Meri Okorie,Vivianne L. Tawfik,John J. Irwin,Alexandros Makriyannis,Georgios Skiniotis,Brian K. Shoichet
标识
DOI:10.1021/acs.jmedchem.6c00835
摘要
Cannabinoid receptors are both therapeutically attractive and are interesting model systems for structure-based methods. Here we investigated topical questions in library docking using the CB2 receptor. While a CB1R docking campaign found potent but nonselective ligands, here subtype selective ligands were found by targeting polar residues. Hit rates and hit affinities improved with library size, but docking against active and inactive receptor states did not reliably bias toward agonists or antagonists. Cryo-EM structures of two of the new agonists superposed well on the docking predictions. Structure-based optimization led to 10- to 140-fold improvements within three series, consistent with well-behaved ligands. Hit rates with an explicit 2.6 billion molecule library resembled those of an implied 11 billion molecule library from a building-block method, supporting the latter's ability to explore this space, though higher affinities were discovered from the explicit set. Implications for future studies are considered.
科研通智能强力驱动
Strongly Powered by AbleSci AI