Deng Nanjie, Flynn William F, Xia Junchao, Vijayan R S K, Zhang Baofeng, He Peng, Mentes Ahmet, Gallicchio Emilio, Levy Ronald M
Center for Biophysics & Computational Biology/ICMS, Philadelphia, PA, USA.
Department of Chemistry, Brooklyn College, the City University of New York, Brooklyn, NY, 11210, USA.
J Comput Aided Mol Des. 2016 Sep;30(9):743-751. doi: 10.1007/s10822-016-9952-x. Epub 2016 Aug 25.
We describe binding free energy calculations in the D3R Grand Challenge 2015 for blind prediction of the binding affinities of 180 ligands to Hsp90. The present D3R challenge was built around experimental datasets involving Heat shock protein (Hsp) 90, an ATP-dependent molecular chaperone which is an important anticancer drug target. The Hsp90 ATP binding site is known to be a challenging target for accurate calculations of ligand binding affinities because of the ligand-dependent conformational changes in the binding site, the presence of ordered waters and the broad chemical diversity of ligands that can bind at this site. Our primary focus here is to distinguish binders from nonbinders. Large scale absolute binding free energy calculations that cover over 3000 protein-ligand complexes were performed using the BEDAM method starting from docked structures generated by Glide docking. Although the ligand dataset in this study resembles an intermediate to late stage lead optimization project while the BEDAM method is mainly developed for early stage virtual screening of hit molecules, the BEDAM binding free energy scoring has resulted in a moderate enrichment of ligand screening against this challenging drug target. Results show that, using a statistical mechanics based free energy method like BEDAM starting from docked poses offers better enrichment than classical docking scoring functions and rescoring methods like Prime MM-GBSA for the Hsp90 data set in this blind challenge. Importantly, among the three methods tested here, only the mean value of the BEDAM binding free energy scores is able to separate the large group of binders from the small group of nonbinders with a gap of 2.4 kcal/mol. None of the three methods that we have tested provided accurate ranking of the affinities of the 147 active compounds. We discuss the possible sources of errors in the binding free energy calculations. The study suggests that BEDAM can be used strategically to discriminate binders from nonbinders in virtual screening and to more accurately predict the ligand binding modes prior to the more computationally expensive FEP calculations of binding affinity.
我们描述了在2015年D3R大挑战中进行的结合自由能计算,用于对180种配体与热休克蛋白90(Hsp90)的结合亲和力进行盲预测。当前的D3R挑战围绕涉及热休克蛋白(Hsp)90的实验数据集构建,Hsp90是一种ATP依赖的分子伴侣,是重要的抗癌药物靶点。已知Hsp90的ATP结合位点对于准确计算配体结合亲和力是一个具有挑战性的靶点,这是因为结合位点存在依赖于配体的构象变化、有序水分子以及可结合于此位点的配体具有广泛的化学多样性。我们在此的主要重点是区分结合剂与非结合剂。使用BEDAM方法,从Glide对接生成的对接结构开始,对超过3000个蛋白质-配体复合物进行了大规模绝对结合自由能计算。尽管本研究中的配体数据集类似于中期到后期的先导优化项目,而BEDAM方法主要是为早期的命中分子虚拟筛选而开发的,但BEDAM结合自由能评分在针对这个具有挑战性的药物靶点的配体筛选中实现了适度的富集。结果表明,在这个盲测挑战中,对于Hsp90数据集,从对接姿势开始使用基于统计力学的自由能方法(如BEDAM)比经典对接评分函数和像Prime MM-GBSA这样的重新评分方法提供了更好的富集效果。重要的是,在此测试的三种方法中,只有BEDAM结合自由能评分的平均值能够以2.4千卡/摩尔的差距将大量的结合剂与少量的非结合剂区分开来。我们测试的这三种方法都没有对147种活性化合物的亲和力进行准确排序。我们讨论了结合自由能计算中可能的误差来源。该研究表明,BEDAM可在虚拟筛选中策略性地用于区分结合剂与非结合剂,并在进行计算成本更高的结合亲和力FEP计算之前更准确地预测配体结合模式。