Zhipeng Yu1,2, Yang Chen1, Wenzhu Zhao1, Jianrong Li1, Jingbo Liu3, Feng Chen2,4. 1. College of Food Science and Engineering, Bohai University, Jinzhou, PR China. 2. Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University (BTBU), Beijing, PR China. 3. Laboratory of Nutrition and Functional Food, Jilin University, Changchun, PR China. 4. Department of Food Science and Human Nutrition, Clemson University, Clemson, SC, USA.
Abstract
BACKGROUND: In order to circumvent some challenges of the classical approach, the in silico method has been applied to the discovery of angiotensin-converting enzyme (ACE) inhibitory peptides from food proteins. In this study, some convenient and efficient in silico tools were utilized to identify novel ACE inhibitory peptides from Salmo salar. RESULTS: Collagen from Salmo salar was digested in silico into hundreds of peptides. Results revealed that tetrapeptides PGAR and IGPR showed potent ACE inhibitory activity, with IC50 values of 0.598 ± 0.12 and 0.43 ± 0.09 mmol L-1 , respectively. The molecular docking result showed that PGAR and IGPR interact with ACE mostly via hydrogen bonds and attractive charge. Peptide IGPR interacts with Zn+ at the ACE active site, showing high inhibitory activity. CONCLUSION: Interaction with Zn+ in ACE may lead to higher inhibitory activity of peptides, and Pi interactions may promote the effect of peptides on ACE. The in silico method can be an effective method to predict potent ACE inhibitory peptides from food proteins.
BACKGROUND: In order to circumvent some challenges of the classical approach, the in silico method has been applied to the discovery of angiotensin-converting enzyme (ACE) inhibitory peptides from food proteins. In this study, some convenient and efficient in silico tools were utilized to identify novel ACE inhibitory peptides from Salmo salar. RESULTS: Collagen from Salmo salar was digested in silico into hundreds of peptides. Results revealed that tetrapeptides PGAR and IGPR showed potent ACE inhibitory activity, with IC50 values of 0.598 ± 0.12 and 0.43 ± 0.09 mmol L-1 , respectively. The molecular docking result showed that PGAR and IGPR interact with ACE mostly via hydrogen bonds and attractive charge. Peptide IGPR interacts with Zn+ at the ACE active site, showing high inhibitory activity. CONCLUSION: Interaction with Zn+ in ACE may lead to higher inhibitory activity of peptides, and Pi interactions may promote the effect of peptides on ACE. The in silico method can be an effective method to predict potent ACE inhibitory peptides from food proteins.
Authors: Mohammad Zarei; Najib Bin Zainal Abidin; Shehu Muhammad Auwal; Shyan Yea Chay; Zaibunnisa Abdul Haiyee; Adi Md Sikin; Nazamid Saari Journal: Biomolecules Date: 2019-10-04