The extreme N-terminal region of human apolipoprotein A-I has a strong propensity to form amyloid fibrils

The N-terminal 1-83 residues of apolipoprotein A-I (apoA-I) have a strong propensity to form amyloid fibrils, in which the 46-59 segment was reported to aggregate to form amyloid-like fibrils. In this study, we demonstrated that a fragment peptide comprising the extreme N-terminal 1-43 residues strongly forms amyloid fibrils with a transition to beta-sheet-rich structure, and that the G26R point mutation enhances the fibril formation of this segment. Our results suggest that in addition to the 46-59 segment, the extreme N-terminal region plays a crucial role in the development of amyloid fibrils by the N-terminal fragment of amyloidogenic apoA-I variants. Structured summary of protein interactions: apoA-I and apoA-I bind by fluorescence technology (1, 2, 3) apoA-I and apoA-I bind by atomic force microscopy (View interaction) apoA-I and apoA-I bind by dynamic light scattering (1, 2) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.