Alzheimer’s disease
acetylcholine
acetylcholinesterase
inhibition
interaction
kinetics
molecular docking
peptide
Journal
Frontiers in nutrition
ISSN: 2296-861X
Titre abrégé: Front Nutr
Pays: Switzerland
ID NLM: 101642264
Informations de publication
Date de publication:
2022
2022
Historique:
received:
23
08
2022
accepted:
07
10
2022
entrez:
7
11
2022
pubmed:
8
11
2022
medline:
8
11
2022
Statut:
epublish
Résumé
Compounds with structural similarities to the neurotransmitter (acetylcholine) are mostly used to inhibit the activity of acetylcholinesterase (AChE) in Alzheimer's disease (AD) therapy. However, the existing drugs only alleviate symptoms of moderate to mild conditions and come with side effects; hence, the search is still on for potent and safer options. In this study, High performance liquid chromatography (HPLC) fractionations of AChE-inhibitory pea protein hydrolysates obtained from alcalase, flavourzyme and pepsin digestions were carried out followed by sequence identification of the most active fractions using mass spectrometry. Subsequently, 20 novel peptide sequences identified from the active fractions were synthesized and five peptides, QSQS, LQHNA, SQSRS, ETRSQ, PQDER (IC
Identifiants
pubmed: 36337665
doi: 10.3389/fnut.2022.1021893
pmc: PMC9635817
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1021893Informations de copyright
Copyright © 2022 Asen, Okagu, Udenigwe and Aluko.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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