SEISAN KENKYU
Online ISSN : 1881-2058
Print ISSN : 0037-105X
ISSN-L : 0037-105X
Volume 62 , Issue 5
Showing 1-17 articles out of 17 articles from the selected issue
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  • Keiichi EDAGAWA, Shigeki IMAGAWA, Keisuke MORITA, Toshiki NIINO
    2010 Volume 62 Issue 5 Pages 557-563
    Published: September 01, 2010
    Released: April 16, 2011
    JOURNAL FREE ACCESS
    Recently, an amorphous structure named “photonic amorphous diamond (PAD)” has been found by numerical calculations to form a sizable three-dimensional photonic band-gap (3D-PBG), despite the complete absence of lattice periodicity. In this article, we review our recent experimental study on the 3D-PBG formation and light propagation properties in PAD.
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  • Takayasu KAWASAKI, Kenjii ONODERA, Shunsuke KAMIJO
    2010 Volume 62 Issue 5 Pages 565-570
    Published: September 01, 2010
    Released: April 16, 2011
    JOURNAL FREE ACCESS
    There have been many reports suggesting that soluble oligomers of amyloid β (Aβ) are neurotoxins causing Alzheimer's disease (AD). Although inhibition of the soluble oligomerization of Aβ is considered to be effective in the treatment of AD, almost all peptide inhibitors have been designed from the β-sheet structure (H14-D23) of Aβ1-42. To obtain more potent peptides than the known inhibitors of the soluble-oligomer formation of Aβ1-42, we performed random screening by phage display. After fifth-round panning of a hepta-peptide library against soluble Aβ1-42, novel peptides containing arginine residues were enriched. These peptides were found to suppress specifically 37/48 kDa oligomer formation and to keep the monomeric form of Aβ1-42 even after 24 h of incubation, as disclosed by SDS-PAGE and size-exclusion chromatography. Thus we succeeded in acquiring novel efficient peptides for inhibition of soluble 37/48 kDa oligomer formation of Aβ1-42.
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