Synthetic peptides corresponding to alpha-lactalbumin and beta-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity.
Novel angiotensin-I-converting enzyme (ACE) inhibitory activities were detected in synthetic peptides corresponding to sequences of beta-lactoglobulin and alpha-lactalbumin and which are known to possess opioid activity. Using hippuryl-histidyl-leucine as substrate, the tetrapeptides beta-lactorphin (Tyr-Leu-Leu-Phe), alpha-lactorphin (Tyr-Gly-Leu-Phe) and beta-lactotensin (His-Ile-Arg-Leu) were shown to have IC50 values of 171.8, 733.3 and 1153.2 microM, respectively. Related dipeptides also inhibited ACE, with Tyr-Leu being the most potent, having an IC50 value of 122.1 microM.
Mullally
M M
MM
National Dairy Products Research Centre, Fermoy, Co. Cork, Ireland.
Meisel
H
H
FitzGerald
R J
RJ
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D002364:Caseins / Q000737:chemistry; D004151:Dipeptides / Q000494:pharmacology; D007768:Lactalbumin / Q000737:chemistry*; D007782:Lactoglobulins / Q000737:chemistry*; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*
D000806:Angiotensin-Converting Enzyme Inhibitors; D002364:Caseins; D004151:Dipeptides; D007782:Lactoglobulins; D009842:Oligopeptides; C102984:beta-lactotensin; C102982:alpha-lactorphin; C102983:beta-lactorphin; C031703:tyrosylleucine; D007768:Lactalbumin