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Updated: Apr 29, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II
Published on: June 16, 2019
Naturally occurring angiotensin I-converting enzyme inhibitory peptide from a fertilized egg and its inhibitory
Xiang Duan1, Fengfeng Wu, Mei Li
1State Key Laboratory of Food Science and Technology, and ‡School of Food Science and Technology, Jiangnan University , 1800 Lihu Road, Wuxi Jiangsu 214122, People's Republic of China.
Abstract:
This study was performed to investigate the angiotensin I-converting enzyme (ACE) inhibitory activity of peptides derived from fertilized eggs and elucidate the inhibition mechanism of these peptides. During incubation, ACE inhibitory activity of the peptides remained stable before day 12 and then increased markedly on day 15. Two ACE inhibitory peptides, VGVIKAVDKKAGGAGKVT and HLFGPPGKKDPV, were purified from peptides on day 15 by consecutive chromatography. Because HLFGPPGKKDPV possessed a higher ACE inhibitory activity (IC50 = 125 μM), an antihypertensive effect of this peptide was further evaluated in vivo. The result showed that this peptide had an antihypertensive effect in spontaneously hypertensive rats (SHRs) at a dosage of 10 mg/kg. Furthermore, Lineweaver-Burk plots suggested that HLFGPPGKKDPV played as a non-competitive inhibitor against ACE, as supported by docking simulation. These data indicated that a fertilized egg has potential as antihypertensive components in functional foods and nutraceuticals.
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