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The extreme N‐terminal region of human apolipoprotein A‐I has a strong propensity to form amyloid fibrils
Author(s) -
Adachi Emi,
Kosaka Asako,
Tsuji Kohei,
Mizuguchi Chiharu,
Kawashima Hiroyuki,
Shigenaga Akira,
Nagao Kohjiro,
Akaji Kenichi,
Otaka Akira,
Saito Hiroyuki
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.11.031
Subject(s) - amyloid fibril , apolipoprotein b , chemistry , amyloid (mycology) , terminal (telecommunication) , fibril , biophysics , biochemistry , amyloid β , medicine , biology , computer science , cholesterol , disease , inorganic chemistry , telecommunications
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.