원문정보
초록
영어
Human intestinal maltase (HMA) is one of these key enzymes that responsible for catalyzing the last glucose-releasing step in starch digestion and it is an important inhibition target in the treatment of type II diabetes. With three dimension structural information of HMA (PDB code: 2QMJ and 2QLY)1 with acarbose as know inhibitor was available and compare the Cα, the HMA was carried out redocking with three parameters and parameter 2 with change of maximum of energy evaluations (ga_num_evals) 2500000 satisfied with -12.62 kcal/mol and RMSD 2.02 A0 and check time to finish one docking lower than 60 minutes. This parameter was chosen for large scale docking on WISDOM production environment2. The result of data challenge showed that 7,977 compounds had lower energy than that of acarbose with energy varied up to -17.09 kcal /mol. All of this data challenge was finished at 3.2 days on 4,700 CPUs with distribution efficiency 54.4%. From 2,974 compounds that had lower energy from -13 kcal/mol were checked hydrogen interaction with key residues of HMA and 87% of compounds showed the interaction with key residue of HMA and 74 select compounds were divided into 17 groups.