Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate.
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.
Miyoshi
S
S
Research and Development Center, Showa Sangyo Co., Ltd., Chiba, Japan.
Ishikawa
H
H
Kaneko
T
T
Fukui
F
F
Tanaka
H
H
Maruyama
S
S
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology; D000818:Animals; D007022:Hypotension / Q000139:chemically induced; D008297:Male; D008969:Molecular Sequence Data; D010455:Peptides / Q000302:isolation & purification / Q000494:pharmacology; D011817:Rabbits; D051381:Rats; D011918:Rats, Inbred SHR; D013329:Structure-Activity Relationship; D015028:Zein / Q000737:chemistry*
D000806:Angiotensin-Converting Enzyme Inhibitors; D010455:Peptides; D015028:Zein