Taira Junichi, Morita Koji, Kawashima Shotaro, Umei Tomohiro, Baba Hiroki, Maruoka Taira, Komatsu Hideyuki, Sakamoto Hiroshi, Sacchettini James C, Aoki Shunsuke
Department of Bioscience and Bioinformatics, Graduate School of Computer Science and Systems Engineering, Kyushu Institute of Technology, Iizuka, Japan.
Department of Biochemistry & Biophysics, Texas A&M University, College Station, Texas, USA.
J Antibiot (Tokyo). 2017 Nov;70(11):1057-1064. doi: 10.1038/ja.2017.106. Epub 2017 Sep 27.
The enzymes responsible for biotin biosynthesis in mycobacteria have been considered as potential drug targets owing to the important role in infection and cell survival that the biotin synthetic pathway plays in Mycobacterium tuberculosis. Among the enzymes that comprise mycobacterium biotin biosynthesis systems, 7,8-diaminopelargonic acid synthase (DAPAS) plays an essential role during the stationary phase in bacterial growth. In this study, compounds that inhibit mycobacterial DAPAS were screened in the virtual chemical library using an in silico structure-based drug screening (SBDS) technique, and the antimycobacterial activity of the selected compounds was validated experimentally. The DOCK-GOLD programs utilized by in silico SBDS facilitated the identification of a compound, referred to as KMD6, with potent inhibitory effects on the growth of model mycobacteria (M. smegmatis). The subsequent compound search, which was based on the structural features of KMD6, resulted in identification of three additional active compounds, designated as KMDs3, KMDs9 and KMDs10. The inhibitory effect of these compounds was comparable to that of isoniazid, which is a first-line antituberculosis drug. The high antimycobacterial activity of KMD6, KMDs9 and KMDs10 was maintained on the experiment with M. tuberculosis. Of the active compounds identified, KMDs9 would be a promising pharmacophore, owing to its long-term antimycobacterial effect and lack of cytotoxicity.
由于生物素合成途径在结核分枝杆菌的感染和细胞存活中发挥着重要作用,因此分枝杆菌中负责生物素生物合成的酶被视为潜在的药物靶点。在构成分枝杆菌生物素生物合成系统的酶中,7,8-二氨基壬酸合酶(DAPAS)在细菌生长的稳定期起着至关重要的作用。在本研究中,使用基于计算机结构的药物筛选(SBDS)技术在虚拟化学库中筛选了抑制分枝杆菌DAPAS的化合物,并通过实验验证了所选化合物的抗分枝杆菌活性。计算机辅助SBDS使用的DOCK-GOLD程序有助于鉴定一种对模型分枝杆菌(耻垢分枝杆菌)生长具有强效抑制作用的化合物,称为KMD6。随后基于KMD6的结构特征进行的化合物搜索,又鉴定出另外三种活性化合物,分别命名为KMDs3、KMDs9和KMDs10。这些化合物的抑制作用与一线抗结核药物异烟肼相当。KMD6、KMDs9和KMDs10在结核分枝杆菌实验中保持了较高的抗分枝杆菌活性。在所鉴定的活性化合物中,KMDs9因其长期的抗分枝杆菌作用和缺乏细胞毒性,将是一种有前景的药效团。