Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-i-converting enzyme inhibitory activity

Margaret M. Mullally, Hans Meisel, Richard J. Fitzgerald

Research output: Contribution to journalArticlepeer-review

Abstract

Novel angiotensin-l-converting enzyme (ACE) inhibitory activities were detected in synthetic peptides corresponding to sequences of β-lactoglobulin and α-lactalbumin and which are known to possess opioid activity. Using hippuryl-histidyl-leucine as substrate, the tetrapeptides β-lactorphin (Tyr-Leu-Leu-Phe), alactorphin (Tyr-Gly-Leu-Phe) and β-lactotensin (HisIle-Arg-Leu) were shown to have ICso values of 171.8, 733.3 and 1153.2 JAM, respectively. Related dipeptides also inhibited ACE, with Tyr-Leu being the most potent, having an ICso value of 122.1 \M.

Original languageEnglish
Pages (from-to)259-260
Number of pages2
JournalBiological Chemistry Hoppe-Seyler
Volume377
Issue number4
Publication statusPublished - 1996
Externally publishedYes

Keywords

  • IC50
  • Multifunctional bioactivity
  • Nutraceutical
  • Opioid peptides

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