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- W2169352885 abstract "Amyloid β (Aβ), a 39–42 amino acid peptide derived from amyloid precursor protein, is deposited as fibrils in Alzheimer's disease brains, and is considered to play a major role in the pathogenesis of the disease. We have investigated the effects of a water-soluble Zn-phthalocyanine, ZnPc(COONa)8, a macrocyclic compound with near-infrared optical properties, on Aβ fibril formation in vitro. A thioflavin T fluorescence assay showed that ZnPc(COONa)8 significantly inhibited Aβ fibril formation, increasing the lag time and dose-dependently decreasing the plateau level of fibril formation. Moreover, it destabilized pre-formed Aβ fibrils, resulting in an increase in low-molecular-weight species. After fibril formation in the presence of ZnPc(COONa)8, immunoprecipitation of Aβ1-42 using Aβ-specific antibody followed by near-infrared scanning demonstrated binding of ZnPc(COONa)8 to Aβ1-42. A study using the hydrophobic fluorescent probe 8-anilino-1-naphthalenesulfonic acid showed that ZnPc(COONa)8 decreased the hydrophobicity during Aβ1-42 fibril formation. CD spectroscopy showed an increase in the α helix structure and a decrease in the β sheet structure of Aβ1-40 in fibril-forming buffer containing ZnPc(COONa)8. SDS/PAGE and a dot-blot immunoassay showed that ZnPc(COONa)8 delayed the disappearance of low-molecular-weight species and the appearance of higher-molecular-weight oligomeric species of Aβ1-42. A cell viability assay showed that ZnPc(COONa)8 was not toxic to a neuronal cell line (A1), but instead protected A1 cells against Aβ1-42-induced toxicity. Overall, our results indicate that ZnPc(COONa)8 binds to Aβ and decreases the hydrophobicity, and this change is unfavorable for Aβ oligomerization and fibril formation." @default.
- W2169352885 created "2016-06-24" @default.
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- W2169352885 date "2014-12-15" @default.
- W2169352885 modified "2023-10-14" @default.
- W2169352885 title "A carboxylated Zn-phthalocyanine inhibits fibril formation of Alzheimer's amyloid β peptide" @default.
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- W2169352885 doi "https://doi.org/10.1111/febs.13151" @default.
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