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. (C) 2018 Elsevier Inc. All rights reserved.