Wu Bainan, Zhang Ziming, Noberini Roberta, Barile Elisa, Giulianotti Marc, Pinilla Clemencia, Houghten Richard A, Pasquale Elena B, Pellecchia Maurizio
Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
Chem Biol. 2013 Jan 24;20(1):19-33. doi: 10.1016/j.chembiol.2012.10.015.
Fragment-based ligand design (FBLD) approaches have become more widely used in drug discovery projects from both academia and industry, and are even often preferred to traditional high-throughput screening (HTS) of large collection of compounds (>10(5)). A key advantage of FBLD approaches is that these often rely on robust biophysical methods such as NMR spectroscopy for detection of ligand binding, hence are less prone to artifacts that too often plague the results from HTS campaigns. In this article, we introduce a screening strategy that takes advantage of both the robustness of protein NMR spectroscopy as the detection method, and the basic principles of combinatorial chemistry to enable the screening of large libraries of fragments (>10(5) compounds) preassembled on a common backbone. We used the method to identify compounds that target protein-protein interactions.
基于片段的配体设计(FBLD)方法在学术界和工业界的药物发现项目中得到了更广泛的应用,甚至常常比传统的高通量筛选(HTS)大量化合物库(>10^5)更受青睐。FBLD方法的一个关键优势在于,这些方法通常依赖于诸如核磁共振波谱等强大的生物物理方法来检测配体结合,因此不太容易出现常常困扰高通量筛选结果的假象。在本文中,我们介绍了一种筛选策略,该策略利用蛋白质核磁共振波谱作为检测方法的稳健性以及组合化学的基本原理,以实现对预先组装在共同骨架上的大量片段库(>10^5化合物)的筛选。我们使用该方法来鉴定靶向蛋白质-蛋白质相互作用的化合物。