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Aβ1-40 mediated aggregation of proteins and metabolites unveils the relevance of amyloid cross-seeding in amyloidogenesis.

Abstract：

:The multicomponent nature of neuronal plaques in Alzheimer's disease signifies the possible recruitment of non-Aβ candidates during the amyloid growth of Aβ peptides. Here, we show that amyloid fibrils of Aβ1-40 peptide can effectively initiate amyloid formation in different globular proteins and metabolites, converting native structures into β-sheet rich assemblies. Structural and biophysical properties of the resultant protein fibrils display amyloid like characteristic features. Viable contacts between Aβ peptide's cross-β architecture and the native structure of proteins, mediated through H-bonds and hydrophobic interactions seem crucial for the onset of amyloid cross-seeding. Results reveal the inherent cross-seeding potential of Aβ amyloids to initiate amyloid formation process in proteins and metabolites and revelation of such a property may further our mechanistic understanding of amyloid pathologies.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Anand BG,Prajapati KP,Kar K

doi

10.1016/j.bbrc.2018.04.198

subject

Has Abstract

pub_date

2018-06-18 00:00:00

pages

158-164

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(18)30995-1

journal_volume

501

pub_type

杂志文章

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