Novel membrane peptidase inhibitory peptides with activity against angiotensin converting enzyme and dipeptidyl peptidase IV identified from hen eggs

被引:55
|
作者
Zhao, Wenzhu [1 ]
Zhang, Dan [1 ]
Yu, Zhipeng [1 ]
Ding, Long [2 ]
Liu, Jingbo [3 ]
机构
[1] Bohai Univ, Coll Food Sci & Engn, Jinzhou 121013, Peoples R China
[2] Northwest A&F Univ, Coll Food Sci & Engn, Yangling 712100, Shaanxi, Peoples R China
[3] Jilin Univ, Lab Nutr & Funct Food, Changchun 130062, Peoples R China
关键词
Angiotensin converting enzyme inhibitory peptides; Dipeptidyl peptidase IV inhibitory peptides; Virtual screening; Molecular docking; IN-SILICO ANALYSIS; BIOACTIVE PEPTIDES; BIOCHEMICAL-CHARACTERIZATION; POTENTIAL PRECURSOR; MOLECULAR-MECHANISM; PROTEIN; PURIFICATION; HYDROLYSATE;
D O I
10.1016/j.jff.2019.103649
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Angiotensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) are important membrane peptidases. The inhibition of ACE and DPP-IV enzymes has become a key therapeutic target for the treatment of hypertension and diabetes. This study was conducted to discover membrane peptidase inhibitory peptides that inhibit ACE and DPP-IV. Egg proteins were cleaved by pepsin and trypsin in silico. The potential activity, solubility, absorption, distribution, metabolism, excretion, and toxicity of the peptides were then predicted online. Finally, ACE and DPP-IV were applied as molecular docking targets for the potential peptides. After simulating gastrointestinal digestion, the IC50 values of ADF, MIR, and FGR against ACE activity were 27.75 +/- 0.90 mM, 24.97 +/- 0.80 mM, and 66.98 +/- 1.40 mu M, against DPP-IV activity were 16.83 mM, 4.86 mM, and 46.22 mM, respectively. The ACE and DPP-IV inhibitory peptides identified from hen egg proteins can be used as functional food ingredients for controlling hypertension and diabetes.
引用
收藏
页数:11
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