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Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway

The elucidation of amyloid nucleation mechanisms remains challenging as early oligomeric intermediates are transient and difficult to distinguish. Here the authors use Aβ- polyglutamine hybrid peptides designed to slow and limit amyloid maturation to provide insights into the structures of Aβ self-assembly intermediates.

Pinaki Misra
Ravindra Kodali
Ronald Wetzel
ResearchOpen Access22 Aug 2016
Nature Communications

Volume: 7, P: 1-15
Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent

The formation of aggregates of polyglutamine (polyQ) sequences is initiated by nucleated growth polymerization. New results show that over a short repeat length range from Q26 to Q23 the size of the nucleus changes from monomeric to dimeric to tetrameric, suggesting aggregation nucleus size has a role in pathogenicity.

Karunakar Kar
Murali Jayaraman
Ronald Wetzel
Research13 Feb 2011
Nature Structural & Molecular Biology

Volume: 18, P: 328-336
Eugenol prevents amyloid formation of proteins and inhibits amyloid-induced hemolysis

Kriti Dubey
Bibin G. Anand
Karunakar Kar
ResearchOpen Access01 Feb 2017
Scientific Reports

Volume: 7, P: 1-11
Intrinsic property of phenylalanine to trigger protein aggregation and hemolysis has a direct relevance to phenylketonuria

Bibin G. Anand
Kriti Dubey
Karunakar Kar
ResearchOpen Access11 Sept 2017
Scientific Reports

Volume: 7, P: 1-9

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Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway

Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent

Eugenol prevents amyloid formation of proteins and inhibits amyloid-induced hemolysis

Intrinsic property of phenylalanine to trigger protein aggregation and hemolysis has a direct relevance to phenylketonuria

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