Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate

Agric Biol Chem. 1991 May;55(5):1313-8.

Abstract

Peptides that inhibit angiotensin-converting enzyme (ACE) were isolated from alpha-zein hydrolysate prepared with thermolysin. Their chemical structures were identified by Edman degradation and fast-atom bombardment mass spectrometry. Most of them were found to be tripeptides such as Leu-Arg-Pro, Leu-Ser-Pro, and Leu-Gln-Pro, having IC50 values of 0.27, 1.7, and 1.9 microM, respectively. These peptides were synthesized by a solid phase procedure and had similar ACE inhibitory activities as the isolated inhibitors. The hypotensive activity of Leu-Arg-Pro on spontaneously hypertensive rats was also investigated, with the result that the the blood pressure decreased by 15 mmHg after a 30 mg/kg intravenous injection.

MeSH terms

  • Amino Acid Sequence
  • Angiotensin-Converting Enzyme Inhibitors / isolation & purification*
  • Angiotensin-Converting Enzyme Inhibitors / pharmacology
  • Animals
  • Hypotension / chemically induced
  • Male
  • Molecular Sequence Data
  • Peptides / isolation & purification
  • Peptides / pharmacology
  • Rabbits
  • Rats
  • Rats, Inbred SHR
  • Structure-Activity Relationship
  • Zein / chemistry*

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Peptides
  • Zein