Modulating Aβ aggregation by tyrosol-based ligands: The crucial role of the catechol moiety.


Journal

Biophysical chemistry
ISSN: 1873-4200
Titre abrégé: Biophys Chem
Pays: Netherlands
ID NLM: 0403171

Informations de publication

Date de publication:
10 2020
Historique:
received: 07 04 2020
revised: 30 06 2020
accepted: 12 07 2020
pubmed: 25 7 2020
medline: 11 5 2021
entrez: 25 7 2020
Statut: ppublish

Résumé

The abnormal deposition of Aβ amyloid deposits in the brain is a hallmark of Alzheimer's disease (AD). Based on this evidence, many current therapeutic approaches focus on the development of small molecules halting Aβ aggregation. However, due to the temporary and elusive structures of amyloid assemblies, the rational design of aggregation inhibitors remains a challenging task. Here we combine ThT assays and MD simulations to study Aβ aggregation in the presence of the natural compounds tyrosol (TY), 3-hydroxytyrosol (HDT), and 3-methoxytyrosol (homovanillyl alcohol - HVA). We show that albeit HDT is a potent inhibitor of amyloid growth, TY and HVA catalyze fibril formation. An inspection of MD simulations trajectories revealed that the different effects of these three molecules on Aβ

Identifiants

pubmed: 32707474
pii: S0301-4622(20)30142-3
doi: 10.1016/j.bpc.2020.106434
pii:
doi:

Substances chimiques

Amyloid beta-Peptides 0
Catechols 0
Ligands 0
Peptide Fragments 0
amyloid beta-protein (1-40) 0
amyloid beta-protein (1-42) 0
homovanillic alcohol 0
4-hydroxyphenylethanol 1AK4MU3SNX
catechol LF3AJ089DQ
Phenylethyl Alcohol ML9LGA7468
Homovanillic Acid X77S6GMS36

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

106434

Informations de copyright

Copyright © 2020 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Valeria Romanucci (V)

Department of Chemical Sciences, University of Naples Federico II, Via Cintia 4, I-80126 Napoli, Italy.

Sara García-Viñuales (S)

Consiglio Nazionale delle Ricerche Istituto di Cristallografia, Via Paolo Gaifami 18, 95126 Catania, Italy.

Carmelo Tempra (C)

Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovonám. 542/2, CZ-16610 Prague, Czech Republic.

Roberta Bernini (R)

Department of Agriculture and Forest Science (DAFNE), University of Tuscia, Via S. Camillo De Lellis, 01100 Viterbo, Italy.

Armando Zarrelli (A)

Department of Chemical Sciences, University of Naples Federico II, Via Cintia 4, I-80126 Napoli, Italy.

Fabio Lolicato (F)

Heidelberg University Biochemistry Center, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany; Department of Physics, University of Helsinki, P.O. Box 64, FI-00014 Helsinki, Finland. Electronic address: Fabio.lolicato@bzh.uni-heidelberg.de.

Danilo Milardi (D)

Consiglio Nazionale delle Ricerche Istituto di Cristallografia, Via Paolo Gaifami 18, 95126 Catania, Italy. Electronic address: danilo.milardi@cnr.it.

Giovanni Di Fabio (G)

Department of Chemical Sciences, University of Naples Federico II, Via Cintia 4, I-80126 Napoli, Italy. Electronic address: difabio@unina.it.

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Classifications MeSH