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Identification of ovalbumin‐derived peptides as multi‐target inhibitors of AChE, BChE, and BACE1
Author(s) -
Yu Zhipeng,
Dong Wanyi,
Wu Sijia,
Shen Juntong,
Zhao Wenzhu,
Ding Long,
Liu Jingbo,
Zheng Fuping
Publication year - 2020
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.10295
Subject(s) - butyrylcholinesterase , acetylcholinesterase , tripeptide , aché , chemistry , ovalbumin , peptide , inhibitory postsynaptic potential , docking (animal) , pharmacology , biochemistry , enzyme , medicine , immunology , antigen , nursing
Abstract BACKGROUND Alzheimer's disease (AD) is a kind of progressive neurodegenerative disease that affects the elderly. There is no ideal treatment for AD. Thus, the purpose of this study is to identify anti‐AD peptides from ovalbumin. RESULTS The potential tripeptides IEK, LYR, and CIK were selected for molecular docking. The ‘‐CDOCKER_Energy’ values of the best docking positions of the tripeptide IEK, LYR, and CIK interacting with acetylcholinesterase (AChE) were 93.8119, 86.9556 and 73.6370 kcal mol −1 , respectively. The ‘‐CDOCKER_Energy’ values for interaction with butyrylcholinesterase (BChE) were 96.6386, 80.8392, and 87.4341 kcal mol −1 , respectively. Most importantly, the ‘‐CDOCKER_Energy’ values for interaction with β ‐site amyloid precursor protein cleavage enzyme1 (BACE1) were 85.5903, 71.3342, and 68.4290 kcal mol −1 , respectively. Overall, in vitro assay results demonstrated that the peptide CIK exhibited impressive inhibitory activities against AChE, BChE, and BACE1, with half maximal inhibitory concentration (IC 50 ) values of 6.76, 7.72, and 34.48 μmol L −1 , respectively. In particular, CIK can be joined with some peripheral anion sites (PAS) and catalytic sites on AChE, BChE, and BACE1. CONCLUSION Tripeptide CIK can effectively inhibit the activities of AChE, BChE, and BACE1. Tripeptide CIK therefore has the potential to treat AD effectively. © 2020 Society of Chemical Industry