期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 58, 期 11, 页码 6721-6727出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf100899u
关键词
Milk-derived peptides; lactoferrin; LfcinB-derived peptides; hypertension; ACE inhibition; ACE-dependent vasoconstriction; SHR; bioavailability; mechanism of action
资金
- Ministerio de Educacion y Ciencia-FEDER [AGL2007-64672/ALI]
- Consolider Ingenio
- Fun-C-Food
- Instituto de Salud Carlos III [CSD2007-00063, RETICS-RD06/0026/0006]
- Ministerio de Educacion y Ciencia [BES-2005-10382]
A set of eight lactoferricin B (LfcinB)-derived peptides was examined for inhibitory effects on angiotensin I-converting enzyme (ACE) activity and ACE-dependent vasoconstriction, and their hypotensive effect in spontaneously hypertensive rats (SHR). Peptides were derived from different elongations both at the C-terminal and N-terminal ends of the representative peptide LfcinB(20-25), which is known as the LfcinB antimicrobial core. All of the eight LfcinB-derived peptides showed in vitro inhibitory effects on ACE activity with different IC50 values. Moreover, seven of them showed ex vivo inhibitory effects on ACE-dependent vasoconstriction. No clear correlation between in vitro and ex vivo inhibitory effects was found. Only LfcinB(20-25) and one of its fragments, F1, generated after a simulated gastrointestinal digestion, showed significant antihypertensive effects in SHR after oral administration. Remarkably, F1 did not show any effect on ACE-dependent vasoconstriction in contrast to the inhibitory effect showed by LfcinB(20-25). In conclusion, two LfcinB-derived peptides lower blood pressure and exhibit potential as orally effective antihypertensive compounds, yet a complete elucidation of the mechanism(s) involved deserves further ongoing research.
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