Visualizing Super-Diffusion, Oligomerization, and Fibrillation of Amyloid-β Peptide Chains along Tubular Membranes

Published on Oct 19, 2021in ACS Macro Letters6.903
· DOI :10.1021/ACSMACROLETT.1C00541
Yuhang Song (WUT: Wuhan University of Technology), Yu Geng (WUT: Wuhan University of Technology), Lei Shen4
Estimated H-index: 4
(WUT: Wuhan University of Technology)
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Abstract
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2019
1 Author (Nabin Kandel)
References30
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#2Bei Li (WUT: Wuhan University of Technology)H-Index: 1
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The complex self-assembly processes in three dimensions of Alzheimer’s β-peptide (Aβ) amyloid protofibrils into polymorphic mature fibrils, particularly the relative protofibril orientation and pac...
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#1Mengting Tian (WUT: Wuhan University of Technology)H-Index: 5
#2Lei Shen (WUT: Wuhan University of Technology)H-Index: 4
An amyloidosis pathway of Alzheimer’s β-peptide Aβ40 on lipid membranes, the self-coiling of single-stranded protofibrils into thermodynamically stable ring structures, is uncovered. Distinct from ...
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#1Shuai Gong (WUT: Wuhan University of Technology)H-Index: 1
#2Jingjing Liu (WUT: Wuhan University of Technology)H-Index: 3
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In this paper, the mechanism of how surface chirality affects amyloid-β (Aβ) fibrillation was firstly unravelled at the molecular level: chiral surface serves to control the 2D-diffusion and surface residence time of Aβ molecules via the chiral recognition with Aβ to allow precursor Aβ to laterally diffuse and collide with each other for oligomerization and fibrillation. Surface chirality that shortens the surface residence time of Aβ, for example R-cysteine modification with carboxylic, seconda...
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#1Jose Ignacio Gallea (National University of Cordoba)H-Index: 4
#2Ernesto E. Ambroggio (National University of Cordoba)H-Index: 10
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: The amyloid aggregation of the presynaptic protein α-synuclein (AS) is pathognomonic of Parkinson's disease and other neurodegenerative disorders. Physiologically, AS contributes to synaptic homeostasis by participating in vesicle maintenance, trafficking, and release. Its avidity for highly curved acidic membranes has been related to the distinct chemistry of the N-terminal amphipathic helix adopted upon binding to appropriated lipid interfaces. Pathologically, AS populate a myriad of toxic a...
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#1Claudio Soto (University of Texas at Austin)H-Index: 82
#2Sandra Pritzkow (University of Texas at Austin)H-Index: 9
A hallmark event in neurodegenerative diseases (NDs) is the misfolding, aggregation, and accumulation of proteins, leading to cellular dysfunction, loss of synaptic connections, and brain damage. Despite the involvement of distinct proteins in different NDs, the process of protein misfolding and aggregation is remarkably similar. A recent breakthrough in the field was the discovery that misfolded protein aggregates can self-propagate through seeding and spread the pathological abnormalities betw...
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#1Mengting Yang (HUST: Huazhong University of Science and Technology)H-Index: 1
#2Kang Wang (WUT: Wuhan University of Technology)H-Index: 1
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Plasma membranes in the human brain can interact with amyloid β-peptide (1–42; Aβ42) and induce Aβ42 fibrillation, which is considered to be a crucial process underlying the neurotoxicity of Aβ42 and the pathogenesis of Alzheimer’s disease (AD). However, the mechanism of membrane-mediated Aβ42 fibrillation at the molecular level remains elusive. Here we study the role of adsorbed Aβ42 peptides on membrane-mediated fibrillation using supported lipid bilayers of varying phase structures (gel and f...
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#2Yuxi Lin (Sookmyung Women's University)H-Index: 3
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Abstract The misfolding, amyloid aggregation, and fibril formation of intrinsically disordered proteins/peptides (or amyloid proteins) have been shown to cause a number of disorders. The underlying mechanisms of amyloid fibrillation and structural properties of amyloidogenic precursors, intermediates, and amyloid fibrils have been elucidated in detail; however, in-depth examinations on physiologically relevant contributing factors that induce amyloidogenesis and lead to cell death remain challen...
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#2Thomas Surrey (Francis Crick Institute)H-Index: 50
Assembly of the microtubule nucleus is energetically unfavourable and, in vivo, microtubule nucleation requires support, such as a stable template, to stabilize the initial weak interactions between tubulin dimers. Microtubules can also be nucleated in the absence of a template by certain microtubule-associated proteins, which stabilize the nascent nucleation intermediates.
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#1Asa Abeliovich (Columbia University)H-Index: 20
#2Aaron D. Gitler (Stanford University)H-Index: 63
Abstract Parkinson's disease is a debilitating, age-associated movement disorder. A central aspect of the pathophysiology of Parkinson's disease is the progressive demise of midbrain dopamine neurons and their axonal projections, but the underlying causes of this loss are unclear. Advances in genetics and experimental model systems have illuminated an important role for defects in intracellular transport pathways to lysosomes. The accumulation of altered proteins and damaged mitochondria, partic...
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#1J. Paul Taylor (St. Jude Children's Research Hospital)H-Index: 76
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Abstract Amyotrophic lateral sclerosis (ALS) is a progressive and uniformly fatal neurodegenerative disease. A plethora of genetic factors have been identified that drive the degeneration of motor neurons in ALS, increase susceptibility to the disease or influence the rate of its progression. Emerging themes include dysfunction in RNA metabolism and protein homeostasis, with specific defects in nucleocytoplasmic trafficking, the induction of stress at the endoplasmic reticulum and impaired dynam...
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