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 β-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.
Keywords: AFM; ATR; Amyloid fibril; Apolipoprotein A-I; FTIR; HDL; Peptide; Point mutation; ThT; WMF; apoA-I; apolipoprotein A-I; atomic force microscopy; attenuated total reflection; fourier transform infrared spectroscopy; high-density lipoprotein; thioflavinT; wavelength of maximum fluorescence.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.