| Literature DB >> 24316228 |
Emi Adachi1, Asako Kosaka1, Kohei Tsuji1, Chiharu Mizuguchi1, Hiroyuki Kawashima2, Akira Shigenaga1, Kohjiro Nagao1, Kenichi Akaji2, Akira Otaka1, Hiroyuki Saito3.
Abstract
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.Entities:
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
Mesh：
Substances：
Year: 2013 PMID： 24316228 DOI： 10.1016/j.febslet.2013.11.031
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124