Abstract
We have previously reported (Kim et al., J. Dairy Res., 1999, in press) three novel angiotensin-I-converting enzyme (ACE) inhibitory peptides, Tyr-Pro-Glu-Arg, Tyr-Tyr-Pro-Gln-Ile-Met-Gln-Tyr and Asn-Asn-Val-Met-Leu-Gln-Trp, isolated from the tryptic digest of recombinant human αs1-casein. A series of C-terminal di- and tripeptides from these three peptides have now been synthesized and their ACE inhibitory activities have been measured. Among the peptides tested, the tripeptide Leu-Gln-Trp had the highest ACE inhibitory activity (IC50=3.8 μmol l−1).
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