Analysis and Evaluation of the Inhibitory Mechanism of a Novel Angiotensin-I-Converting Enzyme Inhibitory Peptide Derived from Casein Hydrolysate.
Maolin TuHanxiong LiuRuyi ZhangHui ChenFengjiao MaoShuzhen ChengWeihong LuLingjun LiPublished in: Journal of agricultural and food chemistry (2018)
Casein hydrolysates exert various biological activities, and the responsible functional peptides are being identified from them continuously. In this study, the tryptic casein hydrolysate was fractionated by an ultrafiltration membrane (3 kDa), and the peptides were identified by capillary electrophoresis-quadrupole-time-of-flight-tandem mass spectrometry. Meanwhile, in silico methods were used to analyze the toxicity, solubility, stability, and affinity between the peptides and angiotensin-I-converting enzyme (ACE). Finally, a new angiotensin-I-converting enzyme inhibitory (ACEI) peptide, EKVNELSK, derived from αs1-casein (fragment 35-42) was screened. The half maximal inhibitory concentration value of the peptide is 5.998 mM, which was determined by a high-performance liquid chromatography method. The Lineweaver-Burk plot indicated that this peptide is a mixed-type inhibitor against ACE. Moreover, Discovery Studio 2017 R2 software was adopted to perform molecular docking to propose the potential mechanisms underlying the ACEI activity of the peptide. These results indicated that EKVNELSK is a new ACEI peptide identified from casein hydrolysate.
Keyphrases
- high performance liquid chromatography
- tandem mass spectrometry
- molecular docking
- mass spectrometry
- ultra high performance liquid chromatography
- angiotensin converting enzyme
- simultaneous determination
- angiotensin ii
- liquid chromatography
- capillary electrophoresis
- gas chromatography
- solid phase extraction
- small molecule
- small cell lung cancer
- high resolution
- ms ms
- blood pressure
- climate change
- heat shock protein
- single cell
- body composition
- brain metastases