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

Chaoyi Wu; Zehui Yin; Yayu Wang; Xinjiani Chen; Bailei Li; Qin Wang; Liping Yao; Zhen Zhang; Xiaojun Liu; Rongqing Zhang

doi:10.1016/j.heliyon.2024.e28060

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

Heliyon. 2024 Mar 18;10(7):e28060. doi: 10.1016/j.heliyon.2024.e28060. eCollection 2024 Apr 15.

Authors

Chaoyi Wu¹, Zehui Yin¹, Yayu Wang², Xinjiani Chen², Bailei Li², Qin Wang², Liping Yao², Zhen Zhang^{2

3}, Xiaojun Liu^{2

4

3}, Rongqing Zhang^{2

4

3}

Affiliations

¹ Key Laboratory of Freshwater Aquatic Genetic Resources, Shanghai Ocean University, Ministry ofAgriculture, Shanghai, 201306, China.
² Department of Biotechnology and Biomedicine, Yangtze Delta Region Institute of Tsinghua University, Zhejiang, 314000, China.
³ Zhejiang Provincial Key Laboratory of Applied Enzymology, Yangtze Delta Region Institute of Tsinghua University, 705 Yatai Road, Jiaxing, 314006, China.
⁴ Taizhou Innovation Center, Yangtze Delta Region Institute of Tsinghua University, Zhejiang, 318000, China.

Abstract

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 μM, 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.

Keywords: ACE-Inhibitory peptide; Kinetic analysis of inhibition; Molecular docking; Pearl matrix proteins.