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

Author

Adachi, Emi, Kosaka, Asako, Tsuji, Kohei, Mizuguchi, Chiharu, Kawashima, Hiroyuki, Shigenaga, Akira, Nagao, Kohjiro, Akaji, Kenichi, Otaka, Akira, and Saito, Hiroyuki

Subjects
*APOLIPOPROTEIN A, *AMYLOID beta-protein, *N-terminal residues, *POINT mutation (Biology), *FOURIER transform infrared spectroscopy, *ATOMIC force microscopy, *HIGH density lipoproteins
Abstract

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]

Published
2014
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