Selection of Angiotensin I Converting Enzyme Inhibitory Peptides from Enzymatic Hydrolysate of Pinctada martensii Using Surface Plasmon Resonance
Surface plasmon resonance (SPR) technology was used to analyze the binding of the three ultrafiltration fractions of the protein hydrolysate of Pinctada martensii (PHPM) with angiotensin I converting enzyme (ACE) as a protein ligand. The amino acid sequences of the bound peptides were identified by...
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China Food Publishing Company
2025-04-01
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| Series: | Shipin Kexue |
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| Online Access: | https://www.spkx.net.cn/fileup/1002-6630/PDF/2025-46-7-017.pdf |
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| author | XIA Xiaoyu, WEN Caixing, CAO Wenhong, QIN Xiaoming, LI Yujin, LIN Haisheng, CHEN Zhongqin, ZHENG Huina, ZHU Guoping, GAO Jialong |
| author_facet | XIA Xiaoyu, WEN Caixing, CAO Wenhong, QIN Xiaoming, LI Yujin, LIN Haisheng, CHEN Zhongqin, ZHENG Huina, ZHU Guoping, GAO Jialong |
| author_sort | XIA Xiaoyu, WEN Caixing, CAO Wenhong, QIN Xiaoming, LI Yujin, LIN Haisheng, CHEN Zhongqin, ZHENG Huina, ZHU Guoping, GAO Jialong |
| collection | DOAJ |
| description | Surface plasmon resonance (SPR) technology was used to analyze the binding of the three ultrafiltration fractions of the protein hydrolysate of Pinctada martensii (PHPM) with angiotensin I converting enzyme (ACE) as a protein ligand. The amino acid sequences of the bound peptides were identified by mass spectrometry (MS) and those with strong inhibitory potential against ACE were selected and synthesized. The in vitro ACE inhibitory activity and inhibition type of the peptides were studied as well as their interaction with ACE. It was found that the ultrafiltration fraction with a molecular mass of 3 000–5 000 Da had a strong binding signal to ACE. Among the four synthesized ACE inhibitory peptides, SLPWPMKPMNLIE had the lowest 50% inhibitory concentration (IC50) value and bound to the hydrophobic pocket of the C domain in ACE through hydrogen bonding. |
| format | Article |
| id | doaj-art-38d486e6dafa45b1aa05cff7b3f9e4ab |
| institution | OA Journals |
| issn | 1002-6630 |
| language | English |
| publishDate | 2025-04-01 |
| publisher | China Food Publishing Company |
| record_format | Article |
| series | Shipin Kexue |
| spelling | doaj-art-38d486e6dafa45b1aa05cff7b3f9e4ab2025-08-20T02:12:18ZengChina Food Publishing CompanyShipin Kexue1002-66302025-04-0146714315010.7506/spkx1002-6630-20241008-016Selection of Angiotensin I Converting Enzyme Inhibitory Peptides from Enzymatic Hydrolysate of Pinctada martensii Using Surface Plasmon ResonanceXIA Xiaoyu, WEN Caixing, CAO Wenhong, QIN Xiaoming, LI Yujin, LIN Haisheng, CHEN Zhongqin, ZHENG Huina, ZHU Guoping, GAO Jialong0(1. College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China; 2. National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Guangdong Province Engineering Laboratory for Marine Biological Products, Key Laboratory of Advanced Processing of Aquatic Product of Guangdong Higher Education Institution, Zhanjiang 524088, China; 3. College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China)Surface plasmon resonance (SPR) technology was used to analyze the binding of the three ultrafiltration fractions of the protein hydrolysate of Pinctada martensii (PHPM) with angiotensin I converting enzyme (ACE) as a protein ligand. The amino acid sequences of the bound peptides were identified by mass spectrometry (MS) and those with strong inhibitory potential against ACE were selected and synthesized. The in vitro ACE inhibitory activity and inhibition type of the peptides were studied as well as their interaction with ACE. It was found that the ultrafiltration fraction with a molecular mass of 3 000–5 000 Da had a strong binding signal to ACE. Among the four synthesized ACE inhibitory peptides, SLPWPMKPMNLIE had the lowest 50% inhibitory concentration (IC50) value and bound to the hydrophobic pocket of the C domain in ACE through hydrogen bonding.https://www.spkx.net.cn/fileup/1002-6630/PDF/2025-46-7-017.pdfpinctada martensii; angiotensin i converting enzyme inhibitory peptide; surface plasmon resonance; enzymatic inhibition kinetics; molecular docking |
| spellingShingle | XIA Xiaoyu, WEN Caixing, CAO Wenhong, QIN Xiaoming, LI Yujin, LIN Haisheng, CHEN Zhongqin, ZHENG Huina, ZHU Guoping, GAO Jialong Selection of Angiotensin I Converting Enzyme Inhibitory Peptides from Enzymatic Hydrolysate of Pinctada martensii Using Surface Plasmon Resonance Shipin Kexue pinctada martensii; angiotensin i converting enzyme inhibitory peptide; surface plasmon resonance; enzymatic inhibition kinetics; molecular docking |
| title | Selection of Angiotensin I Converting Enzyme Inhibitory Peptides from Enzymatic Hydrolysate of Pinctada martensii Using Surface Plasmon Resonance |
| title_full | Selection of Angiotensin I Converting Enzyme Inhibitory Peptides from Enzymatic Hydrolysate of Pinctada martensii Using Surface Plasmon Resonance |
| title_fullStr | Selection of Angiotensin I Converting Enzyme Inhibitory Peptides from Enzymatic Hydrolysate of Pinctada martensii Using Surface Plasmon Resonance |
| title_full_unstemmed | Selection of Angiotensin I Converting Enzyme Inhibitory Peptides from Enzymatic Hydrolysate of Pinctada martensii Using Surface Plasmon Resonance |
| title_short | Selection of Angiotensin I Converting Enzyme Inhibitory Peptides from Enzymatic Hydrolysate of Pinctada martensii Using Surface Plasmon Resonance |
| title_sort | selection of angiotensin i converting enzyme inhibitory peptides from enzymatic hydrolysate of pinctada martensii using surface plasmon resonance |
| topic | pinctada martensii; angiotensin i converting enzyme inhibitory peptide; surface plasmon resonance; enzymatic inhibition kinetics; molecular docking |
| url | https://www.spkx.net.cn/fileup/1002-6630/PDF/2025-46-7-017.pdf |
| work_keys_str_mv | AT xiaxiaoyuwencaixingcaowenhongqinxiaomingliyujinlinhaishengchenzhongqinzhenghuinazhuguopinggaojialong selectionofangiotensiniconvertingenzymeinhibitorypeptidesfromenzymatichydrolysateofpinctadamartensiiusingsurfaceplasmonresonance |