A beta(1-40) mediated aggregation of proteins and metabolites unveils the relevance of amyloid cross-seeding in amyloidogenesis

作者：Anand Bibin G; Prajapati Kailash P; Kar Karunakar

来源：Biochemical and Biophysical Research Communications, 2018, 501(1): 158-164.

DOI：10.1016/j.bbrc.2018.04.198

• A beta peptide
• Alzheimer's disease
• Cross-seeding
• Coaggregation
• Amyloid aggregation

The multicomponent nature of neuronal plaques in Alzheimer's disease signifies the possible recruitment of non-A beta candidates during the amyloid growth of A beta peptides. Here, we show that amyloid fibrils of A beta(1-40) peptide can effectively initiate amyloid formation in different globular proteins and metabolites, converting native structures into beta-sheet rich assemblies. Structural and biophysical properties of the resultant protein fibrils display amyloid like characteristic features. Viable contacts between A beta peptide's cross-beta 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 A beta amyloids to initiate amyloid formation process in proteins and metabolites and revelation of such a property may further our mechanistic understanding of amyloid pathologies.

• 出版日期2018-6-18