AI Chat Paper
Note: Please note that the following content is generated by AMiner AI. SciOpen does not take any responsibility related to this content.
{{lang === 'zh_CN' ? '文章概述' : 'Summary'}}
{{lang === 'en_US' ? '中' : 'Eng'}}
Chat more with AI
PDF (1.4 MB)
Collect
Submit Manuscript AI Chat Paper
Show Outline
Outline
Show full outline
Hide outline
Outline
Show full outline
Hide outline
Research Article | Open Access

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

Zhipeng Yua,bHui GuoaDavid ShiuanaChensi XiaaWenzhu Zhaoa( )Long DingcFuping Zhengb( )Jingbo Liuc( )
College of Food Science and Engineering, Bohai University, Jinzhou 121013, PR China
Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University (BTBU), Beijing 102488, PR China
Lab of Nutrition and Functional Food, Jilin University, Changchun 130062, PR China

Peer review under responsibility of KeAi Communications Co., Ltd.

Show Author Information

Abstract

The egg white-derived hexapeptide TNGIIR inhibits angiotensin-converting enzyme (ACE) activity in vitro. 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 ACE. In 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 tissue. The 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 mRNA. There was no change in the circulating concentration of fAng Ⅰ, 10 amino acids, but a slight decrease (about 10%) was seen in the concentration of circulating angiotensin Ⅱ with TNGIIR and captopril.

References

[1]

L.G. Navar, Counterpoint: Activation of the intrarenal renin-angiotensin system is the dominant contributor to systemic hypertension, J. Appl. Physiol. 109 (6) (2010) 1998-2000.

[2]

A.H. Yee, J.D. Burns, E.F.M. Wijdicks, Cerebral salt wasting: pathophysiology, diagnosis, and treatment, Neurosurg. Clin. N. Am. 21 (2) (2010) 339-352.

[3]

G.R. Marta, L.E. Lván, L.F. Rosina, et al., Egg white hydrolysates with in vitro biological multiactivities to control complications associated with the metabolic syndrome, Eur. Food Res. Technol. 242 (1) (2016) 61-69.

[4]

Z.C. Riccardo, C. Anna, C. Chiara, et al., Purification and identification of endogenous antioxidant and ACE-inhibitory peptides from donkey milk by multidimensional liquid chromatography and nanoHPLC-high resolution mass spectrometry, Anal. Bioanal. Chem. 408 (20) (2016) 5657-5666.

[5]

G.H. Li, G.W. Le, Y.H. Shi, et al., Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects, Nutr. Res. 24 (7) (2004) 469-486.

[6]

B.A. Murray, R.J. FitzGerald, Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production, Curr. Pharm. Design 13 (8) (2007) 773-791.

[7]

W. Liao, S. Chakrabarti, S.T. Davidge, et al., Modulatory effects of egg white ovotransferrin-derived tripeptide IRW (Ile-Arg-Trp) on vascular smooth muscle cells against angiotensin Ⅱ stimulation, J. Agr. Food Chem. 64 (39) (2016) 7342-7347.

[8]

N. Yamamoto, T. Takano, Antihypertensive peptides derived from milk proteins, Nahrung. 43 (3) (1999) 159-164.

[9]

Z.P. Yu, B.Q. Liu, W.Z. Zhao, et al., Primary and secondary structure of novel ACE-inhibitory peptides from egg white protein, Food Chem. 133 (2) (2012) 315-322.

[10]

Z.P. Yu, W.Z. Zhao, L. Ding, et al., Short- and long-term antihypertensive effect of egg protein-derived peptide QIGLF, J. S. F. A. 97 (2) (2017) 551-555.

[11]

J.P. Wu, R.E. Aluko, A.D. Muir, Improved method for direct high-performance liquid chromatography assay of angiotensin-converting enzyme-catalyzed reactions, J. Chromatogr. A 950 (1-2) (2002) 125-130.

[12]

Z.P. Yu, Y.G. Yin, W.Z. Zhao, et al., Antihypertensive effect of angiotensin-converting enzyme inhibitory peptide RVPSL on spontaneously hypertensive rats by regulating gene expression of the renin-angiotensin System, J. Agr. Food Chem. 62 (4) (2014) 912-917.

[13]

Y.J. Zheng, Y. Li, Y.L. Zhang, et al., Purification, characterization, synthesis, in vitro ACE inhibition and in vivo antihypertensive activity of bioactive peptides derived from oil palm kernel glutelin-2 hydrolysates, J. Funct. Foods 28 (2017) 48-58.

[14]

B. Satyanarayana, J.P. Wu, Transport of IRW, an ovotransferrin-derived antihypertensive peptide, in human intestinal epithelial Caco-2 cells, J. Agr. Food Chem. 61 (7) (2017) 1487-1492.

[15]

G.S. Patten, M.Y. Abeywardena, Effects of antihypertensive agents on intestinal contractility in the spontaneously hypertensive rat: angiotensin receptor system downregulation by losartan, J. Pharmacol. Exp. Ther. 360 (2) (2017) 260-266.

[16]

P.J. Ruchaya, G.F. Speretta, G.T. Blanch, et al., Overexpression of AT2R in the solitary-vagal complex improves baroreflex in the spontaneously hypertensive rat, Neuropeptides. 60 (2016) 29-36.

[17]

T. Ichiki, P.A. Labosky, C. Shiota, et al., Effects on blood pressure and exploratory behaviour of mice lacking angiotensin Ⅱ type-2 receptor, Nature. 377 (6551) (1995) 748-750.

[18]

Z. Li, M. Iwai, L. Wu, et al., Role of AT(2) receptor in the brain in regulation of blood pressure and water intake, Am. J. Physiol-Heart. C. 284 (1) (2003) H116-H121.

[19]

L. Hein, G.S. Barsh, R.E. Pratt, et al., Behavioural and cardiovascular effects of disrupting the angiotensin Ⅱ type-2 receptor in mice, Nature. 377 (6551) (1995) 744-747.

[20]

J. Lu, Y. Sawano, T. Miyakawa, et al., One-week antihypertensive effect of Ile-Gln-Pro in spontaneously hypertensive rats, J. Agr. Food Chem 59 (2) (2010) 559-563.

[21]

J.L. Xie, X.J. Chen, J.J. Wu, et al., Antihypertensive effects, molecular docking study, and isothermal titration calorimetry assay of angiotensin Ⅰ-converting enzyme inhibitory peptides from Chlorella vulgaris, J. Agr. Food Chem. 66 (6) (2018) 1359-1368.

[22]

Q.Y. Wu, J.Q. Jia, H. Yan, et al., A novel angiotensin-I converting enzyme (ACE) inhibitory peptide from gastrointestinal protease hydrolysate of silkworm pupa (Bombyx mori) protein: biochemical characterization and molecular docking study, Peptides. 68 (2015) 17-24.

[23]

O. Abdelhedi, R. Nasri, L. Mora, et al., In silico analysis and molecular docking study of angiotensin Ⅰ-converting enzyme inhibitory peptides from smooth-hound viscera protein hydrolysates fractionated by ultrafiltration, Food Chem. 239 (2018) 453-463.

Food Science and Human Wellness
Pages 52-57
Cite this article:
Yu Z, Guo H, Shiuan D, et al. Interaction mechanism of egg white- derived ACE inhibitory peptide TNGIIR with ACE and its effect on the expression of ACE and AT1 receptor. Food Science and Human Wellness, 2020, 9(1): 52-57. https://doi.org/10.1016/j.fshw.2019.12.009

461

Views

35

Downloads

21

Crossref

N/A

Web of Science

19

Scopus

0

CSCD

Altmetrics

Received: 22 September 2019
Revised: 16 December 2019
Accepted: 23 December 2019
Published: 24 December 2019
© 2020 "Society information".

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Return