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

Highlights: [•] The N-terminal 1–83 residues of apoA-I have a propensity to form amyloid fibrils. [•] ApoA-I 1–43 peptide forms amyloid fibrils with transition to β-sheet-rich structure. [•] The G26R point mutation enhances the fibril formation of apoA-I 1–43 peptide. [•] The extreme N-terminal region plays a crucial role in fibril formation by apoA-I. [ABSTRACT FROM AUTHOR]