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Niu, Z.* ; Gui, X.* ; Feng, S.* ; Reif, B.

Aggregation mechanisms and molecular structures of amyloid-β in Alzheimer's disease.

Chem. Eur. J. 30:e202400277 (2024)
Verlagsversion DOI
Open Access Gold (Paid Option)
Creative Commons Lizenzvertrag
Amyloid plaques are a major pathological hallmark involved in Alzheimer's disease and consist of deposits of the amyloid-β peptide (Aβ). The aggregation process of Aβ is highly complex, which leads to polymorphous aggregates with different structures. In addition to aberrant aggregation, Aβ oligomers can undergo liquid-liquid phase separation (LLPS) and form dynamic condensates. It has been hypothesized that these amyloid liquid droplets affect and modulate amyloid fibril formation. In this review, we briefly introduce the relationship between stress granules and amyloid protein aggregation that is associated with neurodegenerative diseases. Then we highlight the regulatory role of LLPS in Aβ aggregation and discuss the potential relationship between Aβ phase transition and aggregation. Furthermore, we summarize the current structures of Aβ oligomers and amyloid fibrils, which have been determined using nuclear magnetic resonance (NMR) and cryo-electron microscopy (cryo-EM). The structural variations of Aβ aggregates provide an explanation for the different levels of toxicity, shed light on the aggregation mechanism and may pave the way towards structure-based drug design for both clinical diagnosis and treatment.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Korrespondenzautor
Schlagwörter Alzheimer's Disease ; Amyloid-β Peptide ; Liquid-liquid Phase Separation ; Protein Aggregation ; Solid-state Nmr; Liquid Phase-separation; Fibril Structure; Atomic Structures; Stress Granules; Alpha-synuclein; A-beta(1-42); Polymorphism; Peptide; Complexity; Amyloid-beta(1-42)
ISSN (print) / ISBN 0947-6539
e-ISSN 1521-3765
Zeitschrift Chemistry - A European Journal
Quellenangaben Band: 30, Heft: 48, Seiten: , Artikelnummer: e202400277 Supplement: ,
Verlag Wiley
Verlagsort Postfach 101161, 69451 Weinheim, Germany
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
Förderungen Projekt DEAL
Bavarian NMR Center
Helmholtz-Gemeinschaft
German Science Foundation
National Natural Science Foundation of China