a 吉林农业大学食品科学与工程学院 长春 130118;
b 吉林大学理论化学研究所理论化学计算国家重点实验室 长春 130061;
c 吉林大学分子酶学工程教育部重点实验室 长春130023
Study of Homology Modeling and High-throughout Screening of a New Inhibitor of Panax β-AS
Zhan Donglinga, Wang Songb, Han Weiweic, Liu Jingshenga
a College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118;
b State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun 130061;
c Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun 130023
Abstract：β-Amyrin synthase from P ginseng (β-AS) catalyzes the biosynthesis of the cyclization of oxidosqualene into Oleanane-type saponins, thereby reducing the amount of steroid formation. However, the 3D structure of β-AS has not been firmly established. To finding the novel inhibitors, a 3D structure model of β-AS protein was constructed based on the structure of the template human oxidosqualene cyclase. After virtual screening technique of β-AS, a novel natural compound (8442257) has been found with the lowest affinity energy. Then we identify that Leu287 is the most important anchoring residues for binding with 8442257 because it has strong vdW interaction with inhibitor. Ser413 and Trp613 are important residues because they make hydrogen bonds with inhibitor. Our results may be helpful for further experimental investigations.
詹冬玲, 王嵩, 韩葳葳, 刘景圣. 人参β-香树素合成酶同源模建及高通量虚拟筛选抑制剂的研究[J]. 化学学报, 2012, 70(03): 217-222.
Zhan Dongling, Wang Song, Han Weiwei, Liu Jingsheng. Study of Homology Modeling and High-throughout Screening of a New Inhibitor of Panax β-AS. Acta Chimica Sinica, 2012, 70(03): 217-222.