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Food Science and Human Wellness 2020, 9(2): 162-167 https://doi.org/10.1016/j.fshw.2020.01.004
Research Article | Open Access | Issue | Published: 24 January 2020

Biological evaluation and interaction mechanism of beta-site APP cleaving enzyme 1 inhibitory pentapeptide from egg albumin

Show Author's Information Zhipeng Yua,b,  Sijia Wua,  Wenzhu Zhaoa( ),  Long Dingc,  David Shiuana,  Fuping Zhengb( ),  Jianrong Lia( ),  Jingbo Liud( )
College of Food Science and Engineering, National & Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Aquatic Products, 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
College of Food Science and Engineering, Northwest A & F University, Yangling, 712100, PR China
Lab of Nutrition and Functional Food, Jilin University, Changchun, 130062, PR China

Peer review under responsibility of KeAi Communications Co., Ltd

Keywords:
Molecular dynamics, Molecular docking, Alzheimer's disease, BACE1, ADMET prediction, KLPGF
Cite this article:
Yu Z, Wu S, Zhao W, et al. Biological evaluation and interaction mechanism of beta-site APP cleaving enzyme 1 inhibitory pentapeptide from egg albumin. Food Science and Human Wellness, 2020, 9(2): 162-167. https://doi.org/10.1016/j.fshw.2020.01.004
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Abstract Full text About this article

Inhibition of beta-site APP cleaving enzyme1 (BACE1) is one of the most promising therapeutic approaches for Alzheimer's disease. To find natural products for the treatment of Alzheimer's disease, absorption, distribution, metabolism, excretion and toxicity (ADMET) properties and in vitro BACE1 inhibitory activity of the peptides isolated from egg albumin were evaluated. Then, molecular docking and molecular dynamics simulation were used to explain the molecular mechanism of the interactions between BACE1 and peptides. The IC50 value of peptide KLPGF, with satisfactory ADMET properties, against BACE1 was (8.30 ± 0.56) mmol/L. Molecular docking revealed that KLPGF contacted with the residues of BACE1's active sites through twelve hydrogen bonds interactions, two hydrophobic interactions, one electrostatic interaction, and two Pi-cation interactions. The 5 ns molecular dynamics simulations confirmed that the structure of KLPGF with BACE1 was stable. Peptide KLPGF contacted the residues Lys321, Asp228, and Asn233 with stable hydrogen bonds. KLPGF may be a potential anti-BACE1 candidate.


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About this article

Biological evaluation and interaction mechanism of beta-site APP cleaving enzyme 1 inhibitory pentapeptide from egg albumin

Show Author's information Zhipeng Yua,b, Sijia Wua, Wenzhu Zhaoa( ), Long Dingc, David Shiuana, Fuping Zhengb( ), Jianrong Lia( ), Jingbo Liud( )
College of Food Science and Engineering, National & Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Aquatic Products, 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
College of Food Science and Engineering, Northwest A & F University, Yangling, 712100, PR China
Lab of Nutrition and Functional Food, Jilin University, Changchun, 130062, PR China

Peer review under responsibility of KeAi Communications Co., Ltd

Abstract

Inhibition of beta-site APP cleaving enzyme1 (BACE1) is one of the most promising therapeutic approaches for Alzheimer's disease. To find natural products for the treatment of Alzheimer's disease, absorption, distribution, metabolism, excretion and toxicity (ADMET) properties and in vitro BACE1 inhibitory activity of the peptides isolated from egg albumin were evaluated. Then, molecular docking and molecular dynamics simulation were used to explain the molecular mechanism of the interactions between BACE1 and peptides. The IC50 value of peptide KLPGF, with satisfactory ADMET properties, against BACE1 was (8.30 ± 0.56) mmol/L. Molecular docking revealed that KLPGF contacted with the residues of BACE1's active sites through twelve hydrogen bonds interactions, two hydrophobic interactions, one electrostatic interaction, and two Pi-cation interactions. The 5 ns molecular dynamics simulations confirmed that the structure of KLPGF with BACE1 was stable. Peptide KLPGF contacted the residues Lys321, Asp228, and Asn233 with stable hydrogen bonds. KLPGF may be a potential anti-BACE1 candidate.

Keywords: Molecular dynamics, Molecular docking, Alzheimer's disease, BACE1, ADMET prediction, KLPGF

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Publication history

Received: 12 October 2019
Revised: 21 November 2019
Accepted: 15 January 2020
Published: 24 January 2020
Issue date: June 2020

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© 2020 "Society information". Production and hosting by Elsevier B.V. on behalf of KeAi Communications Co., Ltd.

Acknowledgements

Acknowledgements

This work was supported by the National Natural Science Funds of China (No.31901635) and the National Key Research and Development Program of China (2018YFD0400301).

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

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