Catechol derivatives inhibit the fibril formation of amyloid-β peptides

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Author(s)

    • Huong Vu Thi HUONG Vu Thi
    • Division of Chemical Engineering, Department of Engineering Science, Graduate School of Engineering Science, Osaka University
    • UMAKOSHI Hiroshi
    • Division of Chemical Engineering, Department of Engineering Science, Graduate School of Engineering Science, Osaka University
    • GOTO Yuji
    • Institute for Protein Research, Osaka University
    • KUBOI Ryoichi
    • Division of Chemical Engineering, Department of Engineering Science, Graduate School of Engineering Science, Osaka University

Abstract

The inhibition of fibril formation of amyloid β proteins (Aβ) would be attractive therapeutic targets for the treatment of Alzheimer's disease (AD). Dopamine (DA) and other catechol derivatives were used as inhibitory factors for Aβ fibril formation. The fibril formation of Aβ was monitored by Thioflavin T fluorescence, a transmission electron microscopy (TEM) and a total internal reflection fluorescence microscopy (TIRFM). Catechol and its derivatives showed the dose-dependent inhibitory effects on the spontaneous Aβ fibril formation. The inhibitory activity depended on the chemical structure of catechol derivatives both in the presence and absence of the liposome a model of biomembrane. Formation of catechol quinone-conjugated-Aβ adduct by a Schiff-base is a key step for the inhibition effect of Aβ fibril formation.

Journal

  • Journal of bioscience and bioengineering

    Journal of bioscience and bioengineering 109(6), 629-634, 2010-06-25

    The Society for Biotechnology, Japan

References:  33

Cited by:  3

Codes

  • NII Article ID (NAID)
    110007641912
  • NII NACSIS-CAT ID (NCID)
    AA11307678
  • Text Lang
    ENG
  • Article Type
    Journal Article
  • ISSN
    13891723
  • NDL Article ID
    10723195
  • NDL Source Classification
    ZP15(科学技術--化学・化学工業--醗酵・微生物工学)
  • NDL Call No.
    Z53-S65
  • Data Source
    CJP  CJPref  NDL  NII-ELS  Crossref 
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