@article{oai:soar-ir.repo.nii.ac.jp:00003913,
 author = {Sawashita,  Jinko and Kametani,  Fuyuki and Hasegawa,  Kazuhiro and Tsutsumi-Yasuhara,  Shinobu and Zhang,  Beiru and Yan,  Jingmin and Mori,  Masayuki and Naiki,  Hironobu and Higuchi,  Keiichi},
 issue = {10},
 journal = {BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS},
 month = {Oct},
 note = {In mice, amyloidogenic type C apolipoprotein A-II (apoA-II) forms amyloid fibrils in age-associated amyloidosis. To understand the mechanism of amyloid fibril formation by apoA-II, we examined the polymerization of synthetic partial peptides of apoA-II in vitro. None of the partial apoA-II peptides polymerized into amyloid fibrils when tested as a single species mixture. We found a unique mechanism in which N- and C-terminal peptides associated into amyloid fibrils in a 1:1 ratio at pH 2.5. The 11-residue amino acid sequence (6-16), which is a common sequence of type B apoA-II and type C apoA-II proteins in amyloidosis-resistant mice and amyloidosis-susceptible mice, respectively, was critical for polymerization into amyloid fibrils. The 18-residue-long amino acid sequence (48-65) is also necessary for nucleation, but not for the extension phase. These findings suggest that there may be different mechanisms underlying the nucleation and extension phases of apoA-II amyloid fibril formation. We also found that amino acid substitutions between type B apoA-II (Pro5, Val38) and type C apoA-II (Gln5, Ala38) did not affect either phase. The strategy of using synthetic partial peptides of amyloidogenic proteins in vitro is a useful system for understanding amyloid fibril formation and for the development of novel therapies., Article, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS. 1794(10):1517-1529 (2009)},
 pages = {1517--1529},
 title = {Amyloid fibrils formed by selective N-, C-terminal sequences of mouse apolipoprotein A-II},
 volume = {1794},
 year = {2009}
}