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Tytuł pozycji:

Fast green FCF inhibits Aβ fibrillogenesis, disintegrates mature fibrils, reduces the cytotoxicity, and attenuates Aβ-induced cognitive impairment in mice.

Tytuł:
Fast green FCF inhibits Aβ fibrillogenesis, disintegrates mature fibrils, reduces the cytotoxicity, and attenuates Aβ-induced cognitive impairment in mice.
Autorzy:
Liu F; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China. Electronic address: .
Wang W; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
Xuan Z; Ningbo Key Laboratory of Behavioral Neuroscience, Zhejiang Provincial Key Laboratory of Pathophysiology, School of Medicine, Ningbo University, Ningbo 315211, China.
Jiang L; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
Chen B; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
Dong Q; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
Zhao F; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
Cui W; Ningbo Key Laboratory of Behavioral Neuroscience, Zhejiang Provincial Key Laboratory of Pathophysiology, School of Medicine, Ningbo University, Ningbo 315211, China.
Li L; College of Marine and Environmental Science, Tianjin University of Science & Technology, Tianjin 300457, China. Electronic address: lili_.
Lu F; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China. Electronic address: .
Źródło:
International journal of biological macromolecules [Int J Biol Macromol] 2021 Feb 15; Vol. 170, pp. 33-41. Date of Electronic Publication: 2020 Dec 19.
Typ publikacji:
Journal Article
Język:
English
Imprint Name(s):
Publication: Amsterdam : Elsevier
Original Publication: Guildford, Eng., IPC Science and Technology Press.
MeSH Terms:
Amyloid/*antagonists & inhibitors
Amyloid beta-Peptides/*drug effects
Cognitive Dysfunction/*prevention & control
Food Additives/*therapeutic use
Lissamine Green Dyes/*therapeutic use
Neuroprotective Agents/*therapeutic use
Protein Aggregation, Pathological/*prevention & control
Alzheimer Disease/metabolism ; Alzheimer Disease/prevention & control ; Amyloid/drug effects ; Amyloid/toxicity ; Amyloid/ultrastructure ; Amyloid beta-Peptides/chemistry ; Animals ; Cognitive Dysfunction/etiology ; Cognitive Dysfunction/metabolism ; Exploratory Behavior/drug effects ; Food Additives/pharmacology ; Humans ; Hydrogen Bonding ; Lissamine Green Dyes/pharmacology ; Mice ; Microscopy, Atomic Force ; Models, Molecular ; Molecular Dynamics Simulation ; Morris Water Maze Test/drug effects ; Neuroprotective Agents/pharmacology ; Peptide Fragments/chemistry ; Peptide Fragments/drug effects ; Protein Aggregation, Pathological/drug therapy ; Protein Structure, Secondary/drug effects ; Random Allocation ; Static Electricity
Contributed Indexing:
Keywords: Alzheimer's disease; Amyloid-β protein; Food additive; Inhibitor; Molecular dynamics simulations
Substance Nomenclature:
0 (Amyloid)
0 (Amyloid beta-Peptides)
0 (Food Additives)
0 (Lissamine Green Dyes)
0 (Neuroprotective Agents)
0 (Peptide Fragments)
155178-13-5 (amyloid beta-protein (17-42))
3P3ONR6O1S (Fast Green FCF)
Entry Date(s):
Date Created: 20201222 Date Completed: 20210414 Latest Revision: 20210414
Update Code:
20240105
DOI:
10.1016/j.ijbiomac.2020.12.115
PMID:
33352157
Czasopismo naukowe
Fast green FCF (FGF) is often used in foods, pharmaceuticals, and cosmetics. However, little is known about the interactions of FGF with amyloid-β protein (Aβ) associated with Alzheimer's disease. In this study, the inhibitory effects of FGF on Aβ fibrillogenesis, the disruption of preformed Aβ fibrils, the reduction of Aβ-induced cytotoxicity, and the attenuation of Aβ-induced learning and memory impairments in mice were investigated. FGF significantly inhibited Aβ fibrillogenesis and disintegrated the mature fibrils as evidenced by thioflavin T fluorescence and atomic force microscopy studies. Co-incubation of Aβ with FGF greatly reduced Aβ-induced cytotoxicity in vitro. Moreover, FGF showed a protective effect against cognitive impairment in Aβ-treated mice. Molecular dynamics simulations further showed that FGF could synergistically interact with the Aβ17-42 pentamer via electrostatic interactions, hydrogen bonds and π-π interactions, which reduced the β-sheet content, and disordered random coils and bend structures of the Aβ17-42 pentamer. This study offers a comprehensive understanding of the inhibitory effects of FGF against Aβ neurotoxicity, which is critical for the search of effective food additives that can combat amyloid-associated disease.
Competing Interests: Declaration of competing interest The authors declare no competing financial interests.
(Copyright © 2020 Elsevier B.V. All rights reserved.)

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