The first bioactive (angiotensin-converting enzyme-inhibitory) peptide isolated from pearl matrix protein

被引：4

作者：

Wu, Chaoyi ^{[1
]}

Yin, Zehui ^{[1
]}

Wang, Yayu ^{[2
]}

Chen, Xinjiani ^{[2
]}

Li, Bailei ^{[2
]}

Wang, Qin ^{[2
]}

Yao, Liping ^{[2
]}

Zhang, Zhen ^{[2
,4
]}

Liu, Xiaojun ^{[2
,3
,4
]}

Zhang, Rongqing ^{[2
,3
,4
]}

机构：

[1] Shanghai Ocean Univ, Key Lab Freshwater Aquat Genet Resources, Minist Agr, Shanghai 201306, Peoples R China

[2] Tsinghua Univ, Dept Biotechnol & Biomed, Yangtze Delta Reg Inst, Jiaxing 314000, Zhejiang, Peoples R China

[3] Tsinghua Univ, Yangtze Delta Reg Inst, Taizhou Innovat Ctr, Jiaxing 318000, Zhejiang, Peoples R China

[4] Tsinghua Univ, Yangtze Delta Reg Inst, Zhejiang Prov Key Lab Appl Enzymol, 705 Yatai Rd, Jiaxing 314006, Peoples R China

来源：

HELIYON | 2024年 / 10卷 / 07期

基金：

中国国家自然科学基金;

关键词：

ACE -Inhibitory peptide; Kinetic analysis of inhibition; Molecular docking; Pearl matrix proteins; BLOOD-PRESSURE; ACE; PURIFICATION; HYDROLYSATE; IDENTIFICATION; FISH; ANTIOXIDANT; EXPRESSION; COMPONENTS; CASEIN;

D O I：

10.1016/j.heliyon.2024.e28060

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

In this research, we unveil the medical potential of pearls by identifying a novel bioactive peptide within them for the first time. The peptide, termed KKCHFWPFPW, emerges as a pioneering angiotensin I -converting enzyme (ACE) inhibitor, originating from the pearl matrix of Pinctada fucata . Employing quadrupole time -of -flight mass spectrometry, this peptide was meticulously selected and pinpointed. With a molecular weight of 1417.5 Da and a theoretical isoelectric point of 9.31, its inhibitory potency was demonstrated through a half -maximal inhibitory concentration (IC50) of 4.17 mu M, established via high-performance liquid chromatography. The inhibition of ACE by this peptide was found to be competitive, as revealed by Lineweaver - Burk plot analysis, where an increase in peptide concentration correlated with an enhanced rate of ACE inhibition. To delve into the interaction between KKCHFWPFPW and ACE, molecular docking simulations were conducted using the Maestro 2022-1 Glide software, shedding light on the inhibitory mechanism. This investigation suggests that peptides derived from the P. martensii pearl matrix hold promise as a novel source for antihypertensive agents.

引用

页数：11

共 48 条

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