期刊
PEPTIDES
卷 30, 期 10, 页码 1848-1853出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2009.06.031
关键词
ACE-inhibitory peptides; Fermented milk; Simulated gastrointestinal digestion; Antihypertensive activity; Competitive inhibitors
资金
- Instituto Danone, Spain [AGL2007-65035, S-0505/AGR/0153, FUN-C-Food CSD2007-00063]
Physiological digestion plays a key role in the formation and degradation of angiotensin-converting enzyme (ACE)-inhibitory peptides. In this study, we evaluated the impact of a simulated gastrointestinal digestion on the stability of eight peptides previously identified in fermented milk with antihypertensive activity. Two of these identified peptides with sequences LHLPLP and LVYPFPGPIPNSLPQNIPP, possess ACE-inhibitory activity in vitro and anti hypertensive activity in vivo. The results showed that LHLPLP was resistant to digestive enzymes. In contrast, LVYPFPGPIPNSLPQNIPP was totally hydrolyzed and its activity decreased after incubation with pepsin and a pancreatic extract. The peptide LHLPLP was incubated with ACE and was found to be a true inhibitor of the enzyme and to exhibit a competitive inhibitor pattern. A structure-activity relationship study of this peptide was carried out by synthesizing several modified peptides related to the sequence LHLPLP. The substitution of amino acid Leu in the penultimate position by Gly improved the ACE-inhibitory activity twofold and the substitution of Pro at C-terminal position by Arg increased the activity twofold, with an IC50 of LHLPLR as low as 1.8 mu M. (C) 2009 Elsevier Inc. All rights reserved.
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