Abstract OR-14: Fibril Structure and Interface Polymorphism of Amyloid-ß(1-42)

Physical basis of amyloid fibril polymorphism

Polymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based reconstructions from different fibril morphologies formed by a peptide fragment from an amyloidogenic immunoglobulin light chain. The observed fibril morphologies vary in the number and cross-sectional arrangemen...

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Physical basis of amyloid fibril polymorphism

Polymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based reconstructions from different fibril morphologies formed by a peptide fragment from an amyloidogenic immunoglobulin light chain. The observed fibril morphologies vary in the number and cross-sectional arrangemen...

متن کامل

Physical basis of amyloid fibril polymorphism

Polymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based reconstructions from different fibril morphologies formed by a peptide fragment from an amyloidogenic immunoglobulin light chain. The observed fibril morphologies vary in the number and cross-sectional arrangemen...

متن کامل

Discovery and structure activity relationship of small molecule inhibitors of toxic β-amyloid-42 fibril formation.

Increasing evidence implicates Aβ peptides self-assembly and fibril formation as crucial events in the pathogenesis of Alzheimer disease. Thus, inhibiting Aβ aggregation, among others, has emerged as a potential therapeutic intervention for this disorder. Herein, we employed 3-aminopyrazole as a key fragment in our design of non-dye compounds capable of interacting with Aβ42 via a donor-accepto...

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Amyloid fibril polymorphism is under kinetic control.

Self-assembly of proteins into amyloid aggregates displays a broad diversity of morphologies, both at the protofibrillar and final fibrillar species. These polymorphic species can coexist at fixed experimental conditions, and their relative abundance can be controlled by changing the solvent composition, or stirring the solution. However, the extent to which external conditions regulate the equ...

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Abstract OR-14: Fibril Structure and Interface Polymorphism of Amyloid-ß(1-42)

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منابع مشابه

Physical basis of amyloid fibril polymorphism

Physical basis of amyloid fibril polymorphism

Physical basis of amyloid fibril polymorphism

Discovery and structure activity relationship of small molecule inhibitors of toxic β-amyloid-42 fibril formation.

Amyloid fibril polymorphism is under kinetic control.

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