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Interaction mechanism of egg white-derived ace inhibitory peptide TNGIIR with ace and its effect on the expression of ace and AT1 receptor

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Food Science and Human Wellness 2020年第1期9卷 52-57页

作者： Zhipeng Yu Hui Guo David Shiuan Chensi Xia Wenzhu Zhao Long Ding Fuping Zheng Jingbo Liu College of Food Science and Engineering Bohai UniversityJinzhou 121013PR China Beijing Advanced Innovation Center for Food Nutrition and Human Health Beijing Technology and Business University(BTBU)Beijing 102488PR China Lab of Nutrition and Functional Food Jilin UniversityChangchun 130062PR China

The egg white-derived hexapeptide TNGIIR inhibits angiotensin-converting enzyme(ace)activity in *** this work,molecular docking revealed that TNGIIR established hydrogen bonds with the S1(Ala 354),S2(Gln 281,His 513,Tyr 520 and Lys 511)and S1(Glu 162)pockets of *** addition,the potential antihypertensive effect of the oral administration of TNGIIR in spontaneously hypertensive rats(SHR)was investigated,as was the effect of this peptide on the mRNA expression of ace and angiotensin type 1(AT1)and type 2(AT2)receptors in renal *** oral administration of TNGIIR(2,10 and 50 mg/kg)for up to four weeks did not reduce the blood pressure of SHR,in contrast to captopril(10 mg/kg,orally),but attenuated the mRNA expression of ace and AT1 receptor(as did captopril).In contrast,both TNGIIR and captopril enhanced the expression of AT2 receptor *** was no change in the circulating concentration of angiotensin I,but a slight decrease(about 10%)was seen in the concentration of circulating angiotensin II with TNGIIR and captopril.

关键词： Egg white proteins ace inhibitory peptide Gene expression Antihypertensive effect Molecular docking

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维普期刊数据库

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Underlying anti-hypertensive mechanism of the Mizuhopecten yessoensis derived peptide NCW in spontaneously hypertensive rats via widely targeted kidney metabolomics

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Food Science and Human Wellness 2024年第1期13卷 472-481页

作者： Wenjun Xue Wenzhu Zhao Sijia Wu Zhipeng Yu School of Food Science and Engineering Hainan UniversityHaikou 570228China College of Food Science and Engineering Bohai UniversityJinzhou 121013China Lab of Nutrition and Functional Food Jilin UniversityChangchun 130062China

The angiotensin-converting enzyme(ace)inhibitory peptide NCW derived from Mizuhopecten yessoensis has been demonstrated to have significant in vivo anti-hypertensive effects,however,its anti-hypertensive mechanism is still not fully *** study established a UPLC-Q-TRAP-MS/MS-based widely targeted kidney metabolomics approach to explore the changes of kidney metabolic profiles and to clarify the antihypertensive mechanism of peptide NCW in spontaneously hypertensive rats(SHRs).Multivariate statistical analysis indicated that the kidney metabolic profiles were clearly separated between the SHR-NCW and SHRUntreated groups.A total of 85 metabolites were differentially regulated,and 16 metabolites were identified as potential kidney biomarkers,e.g.,3-hydroxybutyrate,malonic acid,deoxycytidine,and L-aspartic *** peptide NCW might regulate kidney metabolic disorder of SHRs to alleviate hypertension by suppressing inflammation and improving nitric oxide production under the regulation of linoleic acid metabolism,folate related pathways,synthesis and degradation of ketone bodies,pyrimidine metabolism,β-alanine metabolism,and retinal metabolism.

关键词： ace inhibitory peptide Kidney Mechanism Metabolomics Spontaneously hypertensive rats

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Identifi cation and characterization of a novel tetrapeptide from enzymatic hydrolysates of Baijiu byproduct

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Food Science and Human Wellness 2022年第6期11卷 1641-1649页

作者： Qiang Wu Changqing Zhong Guirong Zeng Xu Zhang Liping Xiang Chang Wan Yougui Yu College of Food and Chemical Engineering Shaoyang UniversityShaoyang 422000China Department of Cardiovascular Medicine Hunan Provincial People's HospitalChangsha 410005China Hunan Experimental Animal Center Hunan Drug Safety Evaluation and Research CenterLiuyang 410331China

In order to prepare angiotensin I-converting enzyme(ace)inhibitory peptides,distilled spent grains of Chinese strong-flavor Baijiu were hydrolyzed by alcalase followed by papain under optimized conditions.A superior ace inhibitory peptide was separated and purifi ed by ultrafi ltration and high-performance liquid chromatography(HPLC),and its amino acid sequence was further identified as Gln-Gly-Val-Pro(QGVP)by electrospray mass spectrometry(ESI-MS).QGVP formed 6 hydrogen bonds with the active site of ace,which is responsible for reducingα-helix structure content of ace causing subsequent inactivation.M oreover,it showed no significant cytotoxicity toward human umbilical vein endothelial cells(HUVECs),a nd signifi cantly i nduced phosphorylation of endothelial nitric oxide synthase(p-e NOS)and decreased endothelin 1(END1)expression in angiotensin I(Ang I)-treated HUVECs,demonstrating the potential antihypertensive *** peptide QGVP hydrolyzed from distilled spent grain proteins of Chinese strong-fl avor Baijiu was expected to be used as a food ingredient to prevent or co-treat hypertension with other chemical drugs.

关键词： Baijiu Distilled spent grain ace inhibitory peptide Inhibition mechanism

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Characterization of ace inhibitory peptides from Mactra veneriformis Hydrolysate by Nano-Liquid Chromatography Electrospray Ionization Mass Spectrometry(Nano-LC-ESI-MS)and Molecular Docking

Characterization of ACE Inhibitory Peptides from Mactra vene...

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全国第九届海洋生物技术与创新药物学术会议

作者： Rui Liu Yunhan Zhu Jiao Chen Hao Wu Lei Shi Xinzhi Wang Lingchong Wang Jiangsu Key Laboratory of Research and Development in Marine Bio-resource Pharmaceutics Nanjing University of Chinese Medicine National and Local Collaborative Engineering Center of Chinese Medicinal Resources Industrialization and Formulae Innovative Medicine Nanjing University of Chinese Medicine Jiangsu Collaborative Innovation Center of Chinese Medicinal Resources Industrialization Nanjing University of Chinese Medicine College of Pharmacy Nanjing University of Chinese Medicine China Pharmaceutical University

Food-derived bioactive compounds are gaining increasing significance in life *** the present study,we identified angiotensin I-converting enzyme(ace)-inhibitory peptides from Mactra veneriformis hydrolysate using a nano-LC-MS/MS *** veneriformis hydrolysate was first separated into four fractions(F1-F4)based on molecular weight by *** fraction with molecular weight lower than 1 kDa(F1)showed the highest ace inhibitory activity.F1 was then analyzed by a high throughput nano-LC-MS/MS method and sequences of peptides in F1 were calculated *** 27 peptides identified as above were chemically synthesized and tested for ace-inhibitory *** hexapeptide WCVPW showed the highest potency with an ICvalue of 4.07μ*** then investigated the interaction mechanism between the six most potent peptides and ace by molecular *** docking results suggested that the ace inhibitory peptides bind to ace via interactions with His383,His387,and Glu411 ***,similar to the thiol group of captopril,the cysteine thiol group of the most potent peptide WCVPW may play a key role in the binding of this peptide to the ace active site.

关键词： ace inhibitory peptide characterization nano-LC-MS/MS molecular docking Mactra veneriformis

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