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- W1960993458 abstract "Deposition of insoluble fibrillar aggregates of β‐amyloid (Aβ) peptides in the brain is a hallmark of Alzheimer's disease. Apart from forming fibrils, these peptides also exist as soluble aggregates. Fibrillar and a variety of nonfibrillar aggregates of Aβ have also been obtained in vitro . Hexafluoroisopropanol (HFIP) has been widely used to dissolve Aβ and other amyloidogenic peptides. In this study, we show that the dissolution of Aβ40, 42, and 43 in HFIP followed by drying results in highly ordered aggregates. Although α‐helical conformation is observed, it is not stable for prolonged periods. Drying after prolonged incubation of Aβ40, 42, and 43 peptides in HFIP leads to structural transition from α‐helical to β‐conformation. The peptides form short fibrous aggregates that further assemble giving rise to highly ordered ring‐like structures. Aβ16–22, a highly amyloidogenic peptide stretch from Aβ, also formed very similar rings when dissolved in HFIP and dried. HFIP could not induce α‐helical conformation in Aβ16–22, and rings were obtained from freshly dissolved peptide. The rings formed by Aβ40, 42, 43, and Aβ16–22 are composed of the peptides in β‐conformation and cause enhancement in thioflavin T fluorescence, suggesting that the molecular architecture of these structures is amyloid‐like. Our results clearly indicate that dissolution of Aβ40, 42 and 43 and the amyloidogenic fragment Aβ16–22 in HFIP results in the formation of annular amyloid‐like structures. Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd." @default.
- W1960993458 created "2016-06-24" @default.
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- W1960993458 date "2012-01-17" @default.
- W1960993458 modified "2023-10-17" @default.
- W1960993458 title "Hexafluoroisopropanol induces self-assembly of β-amyloid peptides into highly ordered nanostructures" @default.
- W1960993458 cites W1602771322 @default.
- W1960993458 cites W1603138791 @default.
- W1960993458 cites W1830667138 @default.
- W1960993458 cites W1964741226 @default.
- W1960993458 cites W1966694507 @default.
- W1960993458 cites W1967064045 @default.
- W1960993458 cites W1972535964 @default.
- W1960993458 cites W1976317909 @default.
- W1960993458 cites W1976550948 @default.
- W1960993458 cites W1979509752 @default.
- W1960993458 cites W1980825524 @default.
- W1960993458 cites W1981281118 @default.
- W1960993458 cites W1981439495 @default.
- W1960993458 cites W1981735680 @default.
- W1960993458 cites W1982907308 @default.
- W1960993458 cites W1983877884 @default.
- W1960993458 cites W1985089573 @default.
- W1960993458 cites W1987205935 @default.
- W1960993458 cites W1987686455 @default.
- W1960993458 cites W1989270637 @default.
- W1960993458 cites W1989386714 @default.
- W1960993458 cites W1990749733 @default.
- W1960993458 cites W1999206064 @default.
- W1960993458 cites W1999213903 @default.
- W1960993458 cites W2004400100 @default.
- W1960993458 cites W2004605168 @default.
- W1960993458 cites W2005791922 @default.
- W1960993458 cites W2008630616 @default.
- W1960993458 cites W2009046737 @default.
- W1960993458 cites W2015522247 @default.
- W1960993458 cites W2016807968 @default.
- W1960993458 cites W2017014806 @default.
- W1960993458 cites W2019212178 @default.
- W1960993458 cites W2019827191 @default.
- W1960993458 cites W2023531011 @default.
- W1960993458 cites W2033829612 @default.
- W1960993458 cites W2033975469 @default.
- W1960993458 cites W2034254998 @default.
- W1960993458 cites W2035241014 @default.
- W1960993458 cites W2037346440 @default.
- W1960993458 cites W2038618709 @default.
- W1960993458 cites W2039018328 @default.
- W1960993458 cites W2048350253 @default.
- W1960993458 cites W2059035251 @default.
- W1960993458 cites W2059128072 @default.
- W1960993458 cites W2065100984 @default.
- W1960993458 cites W2067214887 @default.
- W1960993458 cites W2073516240 @default.
- W1960993458 cites W2073686561 @default.
- W1960993458 cites W2074619433 @default.
- W1960993458 cites W2075481535 @default.
- W1960993458 cites W2075930760 @default.
- W1960993458 cites W2076767192 @default.
- W1960993458 cites W2080399081 @default.
- W1960993458 cites W2086258145 @default.
- W1960993458 cites W2087748229 @default.
- W1960993458 cites W2091029987 @default.
- W1960993458 cites W2094190981 @default.
- W1960993458 cites W2110588649 @default.
- W1960993458 cites W2117118343 @default.
- W1960993458 cites W2122294662 @default.
- W1960993458 cites W2124607319 @default.
- W1960993458 cites W2126036997 @default.
- W1960993458 cites W2126964809 @default.
- W1960993458 cites W2130786862 @default.
- W1960993458 cites W2133631618 @default.
- W1960993458 cites W2134909516 @default.
- W1960993458 cites W2136163423 @default.
- W1960993458 cites W2155916246 @default.
- W1960993458 cites W2164862888 @default.
- W1960993458 doi "https://doi.org/10.1002/psc.2391" @default.
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