Identification of ACE-inhibitory peptides from Mactra veneriformis hydrolysate by using UPLC-Q-TOF MS coupled to molecular docking
- 作者：Rui LiuYunhan ZhuHao WuSiwei ZhangLingchong WangXinzhi Wang
- 会议时间：2013-10-18
- 关键词：ACE inhibitory peptide ; identification ; UPLC-Q-TOF MS ; Molecular docking ; Mactra veneriformis
- 作者单位：Rui Liu,Yunhan Zhu,Hao Wu,Lingchong Wang,Xinzhi Wang(Jiangsu Key Laboratory of Research and Development in Marine Bio-resource Pharmaceutics,Nanjing University of Chinese Medicine,Nanjing,Jiangsu,210023,China;College of Pharmacy,Nanjing University of Chinese Medicine,Nanjing University of Chinese Medicine,Nanjing,Jiangsu,210023,China)Siwei Zhang(China Pharmaceutical University,Nanjing,Jiangsu,210009,China)
- 母体文献：中国药学会海洋药物专业委员会第十一届海洋药物学术年会论文集
- 会议名称：中国药学会海洋药物专业委员会第十一届海洋药物学术年会
- 会议地点：海口
- 主办单位：中国药学会
- 语种：chi
摘要
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.