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View article: Aducanumab binding to Aβ <sub>1-42</sub> fibrils alters dynamics of the N-terminal tail while preserving the fibril core
Aducanumab binding to Aβ <sub>1-42</sub> fibrils alters dynamics of the N-terminal tail while preserving the fibril core Open
Aducanumab, a human IgG1 antibody with plaque-clearing effects and modest clinical benefit, binds selectively to aggregated Aβ via the N-terminal region. Yet, the molecular details of how the antibody engages Aβ 1-42 fibrils remain unresol…
View article: Aducanumab Binding to Aβ1-42 Fibrils Alters Dynamics of the N-Terminal Tail While Preserving the Fibril Core
Aducanumab Binding to Aβ1-42 Fibrils Alters Dynamics of the N-Terminal Tail While Preserving the Fibril Core Open
Aducanumab, a human IgG1 antibody with plaque-clearing effects and modest clinical benefit, binds selectively to aggregated Aβ via the N-terminal region. Yet, the molecular details of how the antibody engages Aβ 1-42 fibrils remain unresol…
View article: The Role of α-Synuclein–DNAJB6b Coaggregation in Amyloid Suppression
The Role of α-Synuclein–DNAJB6b Coaggregation in Amyloid Suppression Open
Chaperones may retard the aggregation of other proteins and increase their solubility. An important goal is a thermodynamic understanding of such an action. Here, the chaperone DNAJB6b (JB6) is found to suppress amyloid formation of the pr…
View article: On the self-assembly of αB-crystallin
On the self-assembly of αB-crystallin Open
In this work the self-assembly of the chaperone αB-crystallin is shown to follow the closed association model to a good approximation. The oligomeric form is found to consist of 18 monomers, approximately 7 nm in radius, independent of con…
View article: Residues 2 to 7 of α-synuclein regulate amyloid formation via lipid-dependent and lipid-independent pathways
Residues 2 to 7 of α-synuclein regulate amyloid formation via lipid-dependent and lipid-independent pathways Open
Amyloid formation by α-synuclein (αSyn) occurs in Parkinson’s disease, multiple system atrophy, and dementia with Lewy bodies. Deciphering the residues that regulate αSyn amyloid fibril formation will not only provide mechanistic insight b…
View article: The role of shear forces in primary and secondary nucleation of amyloid fibrils
The role of shear forces in primary and secondary nucleation of amyloid fibrils Open
Shear forces affect self-assembly processes ranging from crystallization to fiber formation. Here, the effect of mild agitation on amyloid fibril formation was explored for four peptides and investigated in detail for A 42, which is ass…
View article: Residues 2-7 of α-synuclein regulate amyloid formation via lipid-dependent and -independent pathways
Residues 2-7 of α-synuclein regulate amyloid formation via lipid-dependent and -independent pathways Open
Amyloid formation by α-synuclein (αSyn) occurs in Parkinson’s disease, multiple system atrophy, and dementia with Lewy bodies. Deciphering the residues that regulate αSyn amyloid fibril formation will not only provide mechanistic insight, …
View article: Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces
Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces Open
Oligomeric assemblies consisting of only a few protein subunits are a key species in the cytotoxicity of neurodegenerative disorders, such as Alzheimer’s and Parkinson’s diseases. Their lifetime in solution and their abundance, governed by…
View article: Direct observation of secondary nucleation along the fibril surface of the amyloid <i>β</i> 42 peptide
Direct observation of secondary nucleation along the fibril surface of the amyloid <i>β</i> 42 peptide Open
Alzheimer’s disease is a neurodegenerative condition which involves heavy neuronal cell death linked to oligomers formed during the aggregation process of the amyloid β peptide 42 (A β 42). The aggregation of A β 42 involves both primary a…
View article: A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ <sub>42</sub> Aggregation
A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ <sub>42</sub> Aggregation Open
The aggregation of the amyloid β (Aβ) peptide is one of the molecular hallmarks of Alzheimer's disease (AD). Although Aβ deposits have mostly been observed extracellularly, various studies have also reported the presence of intracellular A…
View article: Role of Hydrophobicity at the N-Terminal Region of Aβ42 in Secondary Nucleation
Role of Hydrophobicity at the N-Terminal Region of Aβ42 in Secondary Nucleation Open
The self-assembly of the amyloid β 42 (Aβ42) peptide is linked to Alzheimer's disease, and oligomeric intermediates are linked to neuronal cell death during the pathology of the disease. These oligomers are produced prolifically during sec…
View article: A Palette of Fluorescent Aβ42 Peptides Labelled at a Range of Surface-Exposed Sites
A Palette of Fluorescent Aβ42 Peptides Labelled at a Range of Surface-Exposed Sites Open
Fluorescence-based single molecule techniques provide important tools towards understanding the molecular mechanism of complex neurodegenerative diseases. This requires efficient covalent attachment of fluorophores. Here we create a series…
View article: The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils
The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils Open
Significance Alzheimer’s disease affects a rapidly growing number of individuals worldwide. Key unresolved questions relate to the onset and propagation of the disease, linked to the self-assembly of amyloid β peptide into fibrillar and sm…