文摘
A selection of lactoferricin B (LfcinB)-related peptides with an angiotensin I-converting enzyme (ACE)inhibitory effect have been examined using in vitro and ex vivo functional assays. Peptides that wereanalyzed included a set of sequence-related antimicrobial hexapeptides previously reported and tworepresentative LfcinB-derived peptides. In vitro assays using hippuryl-L-histidyl-L-leucine (HHL) andangiotensin I as substrates allowed us to select two hexapeptides, PACEI32 (Ac-RKWHFW-NH2)and PACEI34 (Ac-RKWLFW-NH2), and also a LfcinB-derived peptide, LfcinB17-31 (Ac-FKCRRWQWRMKKLGA-NH2). Ex vivo functional assays using rabbit carotid arterial segments showedPACEI32 (both D- and L-enantiomers) and LfcinB17-31 have inhibitory effects on ACE-dependentangiotensin I-induced contraction. None of the peptides exhibited in vitro ACE inhibitory activity usingbradykinin as the substrate. In conclusion, three bioactive lactoferricin-related peptides exhibit inhibitoryeffects on both ACE activity and ACE-dependent vasoconstriction with potential to modulatehypertension that deserves further investigation.Keywords: Lactoferricin B-related peptides; ACE inhibition; ex vivo functional assay; ACE-dependentvasoconstriction