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 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...

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Bibliographic Details
Published in:	FEBS letters Vol. 588; no. 3; pp. 389 - 394
Main Authors:	Adachi, Emi, Kosaka, Asako, Tsuji, Kohei, Mizuguchi, Chiharu, Kawashima, Hiroyuki, Shigenaga, Akira, Nagao, Kohjiro, Akaji, Kenichi, Otaka, Akira, Saito, Hiroyuki
Format:	Journal Article
Language:	English
Published:	England Elsevier B.V 31-01-2014
Subjects:	AFM Amyloid - biosynthesis Amyloid - chemistry Amyloid - genetics Amyloid fibril apoA-I Apolipoprotein A-I Apolipoprotein A-I - biosynthesis Apolipoprotein A-I - chemistry Apolipoprotein A-I - genetics atomic force microscopy ATR attenuated total reflection Circular Dichroism fourier transform infrared spectroscopy FTIR HDL high-density lipoprotein Humans Microscopy, Atomic Force Peptide Peptide Fragments - chemical synthesis Peptide Fragments - chemistry Peptide Fragments - genetics Point Mutation Protein Conformation Protein Structure, Secondary Spectroscopy, Fourier Transform Infrared thioflavinT ThT wavelength of maximum fluorescence WMF HDL ThT WMF FTIR Apolipoprotein A-I Point mutation AFM Amyloid fibril Peptide apoA-I ATR high-density lipoprotein atomic force microscopy attenuated total reflection thioflavinT fourier transform infrared spectroscopy wavelength of maximum fluorescence
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Summary:	•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. 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. apoA-I and apoA-Ibind by fluorescence technology (1, 2, 3) apoA-I and apoA-Ibind by atomic force microscopy (View interaction) apoA-I and apoA-Ibind by dynamic light scattering (1, 2)
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0014-5793 1873-3468
DOI:	10.1016/j.febslet.2013.11.031