Biotechnology Center (BIOTEC), TU Dresden, Dresden, Germany.
PLoS One. 2013 Jun 21;8(6):e65894. doi: 10.1371/journal.pone.0065894. Print 2013.
Drug repositioning applies established drugs to new disease indications with increasing success. A pre-requisite for drug repurposing is drug promiscuity (polypharmacology) - a drug's ability to bind to several targets. There is a long standing debate on the reasons for drug promiscuity. Based on large compound screens, hydrophobicity and molecular weight have been suggested as key reasons. However, the results are sometimes contradictory and leave space for further analysis. Protein structures offer a structural dimension to explain promiscuity: Can a drug bind multiple targets because the drug is flexible or because the targets are structurally similar or even share similar binding sites? We present a systematic study of drug promiscuity based on structural data of PDB target proteins with a set of 164 promiscuous drugs. We show that there is no correlation between the degree of promiscuity and ligand properties such as hydrophobicity or molecular weight but a weak correlation to conformational flexibility. However, we do find a correlation between promiscuity and structural similarity as well as binding site similarity of protein targets. In particular, 71% of the drugs have at least two targets with similar binding sites. In order to overcome issues in detection of remotely similar binding sites, we employed a score for binding site similarity: LigandRMSD measures the similarity of the aligned ligands and uncovers remote local similarities in proteins. It can be applied to arbitrary structural binding site alignments. Three representative examples, namely the anti-cancer drug methotrexate, the natural product quercetin and the anti-diabetic drug acarbose are discussed in detail. Our findings suggest that global structural and binding site similarity play a more important role to explain the observed drug promiscuity in the PDB than physicochemical drug properties like hydrophobicity or molecular weight. Additionally, we find ligand flexibility to have a minor influence.
药物重定位将已上市药物应用于新的疾病适应症,成功率不断提高。药物重定位的前提是药物混杂性(多药理学)——药物结合多个靶点的能力。药物混杂性的原因一直存在争议。基于大规模化合物筛选,疏水性和分子量已被认为是关键原因。然而,结果有时相互矛盾,仍有进一步分析的空间。蛋白质结构为解释混杂性提供了一个结构维度:药物是否可以结合多个靶点,是因为药物具有柔韧性,还是因为靶点在结构上相似,甚至共享相似的结合位点?我们基于 PDB 靶蛋白的结构数据,对 164 种混杂药物进行了系统研究,展示了药物混杂性与配体性质(如疏水性或分子量)之间没有相关性,但与构象柔韧性有弱相关性。然而,我们确实发现药物混杂性与蛋白质靶标结构相似性和结合位点相似性之间存在相关性。特别是,71%的药物至少有两个具有相似结合位点的靶标。为了克服远程相似结合位点检测中的问题,我们采用了结合位点相似性评分:配体 RMSD 衡量配体对齐的相似性,并揭示蛋白质中远程局部相似性。它可应用于任意结构的结合位点对齐。以三种代表性药物为例,即抗癌药物甲氨蝶呤、天然产物槲皮素和抗糖尿病药物阿卡波糖,进行了详细讨论。我们的研究结果表明,全局结构和结合位点相似性比疏水性或分子量等物理化学药物特性对解释 PDB 中观察到的药物混杂性更为重要。此外,我们发现配体柔韧性的影响较小。