Identification of ACE-inhibitory peptides from Mactra veneriformis hydrolysate by using UPLC-Q-TOF MS coupled to molecular docking
Compared with chemical synthetic drugs, food derived bioactive compounds are increasingly become important in life sciences.In present study, ACE-inhibitory peptides were identified from Mactra veneriformis hydrolysate based on UPLC-Q-TOF MS coupled molecular docking method.Ultrafiltration was firstly used for separating hydrolysate into four fractions.The fraction with molecular weight lower than 1 kDa possesses the greatest ACE inhibitory activity.Active fraction then was analyzed by UPLC-Q-TOF MS/MS and sequences of peptides were calculated.Molecular docking was used to investigate the interactions between the calculated peptides and the ACE.Two ACE-inhibitory peptides with amino acid sequences of LASPTM and LL were obtained finally and LASPTM was verified as a potent peptide with an IC50 of 59.81 μM.
ACE inhibitory peptide identification UPLC-Q-TOF MS Molecular docking Mactra veneriformis
Rui Liu Yunhan Zhu Hao Wu Siwei Zhang Lingchong Wang Xinzhi Wang
Jiangsu Key Laboratory of Research and Development in Marine Bio-resource Pharmaceutics,Nanjing Univ China Pharmaceutical University,Nanjing,Jiangsu,210009,China
国内会议
海口
英文
10-18
2013-10-18（万方平台首次上网日期，不代表论文的发表时间）