| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8261584 | Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease | 2012 | 9 Pages |
Abstract
⺠Isoflavones inhibited the fibrillization and oligomerization of amyloid β-proteins (Aβs). ⺠Isoflavones destabilized preformed amyloid β-protein (Aβ) fibrils. ⺠Glycitein bound to Aβ monomers, oligomers and fibrils, leading the anti-amyloidogenic effects. ⺠Glycitein bound to Aβ1-42, Aβ1-40, Aβ1-16 and Aβ25-35, having the most potent affinity for Aβ25-35.
Keywords
AFMDAITTRFormononetinDTTPICUPAβamyloid β-proteinphoto-induced cross-linking of unmodified proteinsEmissionphosphate bufferFORThTAlzheimer's diseaseThioflavine Tstandard errorDaidzeinpurdithiothreitolcircular dichroismThree-dimensional fluorescence spectroscopyFragmentGenisteinCerebrospinal fluidCSFequElectron microscopyatomic force microscopyExcitationArbitrary UnitGENGlyGlycitein
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Ageing
Authors
Mie Hirohata, Kenjiro Ono, Jun-ichi Takasaki, Ryoichi Takahashi, Tokuhei Ikeda, Akiyoshi Morinaga, Masahito Yamada,