期刊
JOURNAL OF FUNCTIONAL FOODS
卷 45, 期 -, 页码 401-408出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jff.2018.04.020
关键词
Bioactive peptide; Angiotensin I-converting enzyme; Permeability; Transepithelial transport; Molecular docking
资金
- Royal Golden Jubilee Scholarship [PhD/0223/2552]
- Suranaree University of Technology (SUT)
- Office of the Higher Education Commission under NRU project of Thailand
- Natural Sciences & Engineering Research Council of Canada research grants
Permeability of angiotensin 1-converting enzyme (ACE) inhibitory peptides (KPLLCS, ELFTT, and KPLL) identified from the in vitro gastrointestinal digest of cooked chicken breast was investigated using the Caco-2 cell model system. KPLLCS was originally the most effective ACE inhibitor (IC50 0.37 mu M), but it was degraded during permeation through Caco-2 cells. Among these peptides, KPLL showed the highest permeability in intact form, and partially degraded to KP and LL, which still showed ACE inhibitory activity after permeation. ACE inhibitory activity of permeated KPLL was highest of 56%. KPLL and KP possessed a mixed inhibitor characteristic, while LL was a non-competitive inhibitor. Based on molecular docking, K at N-terminus of KPLL is a key structure contributing to ACE inhibition as it can occupy the active site of ACE. Determining the structural stability and degree of peptide transport across epithelial cell is required to confirm their potential as ACE inhibitors.
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