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• W2022209862 abstract "The formation of the beta pleated configuration of the amyloid peptide fragment 25-35 in aqueous solution, has been studied using thioflavin-T fluorescence as an indicator of such folding. Both phosphate and adenosine triphosphate (ATP) enhance the formation of aggregated beta-sheets. This phosphate-induced aggregation is greater in the presence of aluminum sulfate in a dose dependent manner. In the absence of ATP or phosphate, aluminum salts do not promote aggregation. It is proposed that a particulate aluminum phosphate complex may form critical nuclei upon whose surface the amyloid peptide can change its configuration. This capacity for seeding may be a relevant factor in the formation of insoluble proteinaceous materials such as amyloid plaques and neurofibrillary tangles found in Alzheimer's disease." @default.
• W2022209862 created "2016-06-24" @default.
• W2022209862 creator A5063352695 @default.
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• W2022209862 date "1999-05-01" @default.
• W2022209862 modified "2023-09-23" @default.
• W2022209862 title "Potentiation of beta-folding of β-amyloid peptide 25–35 by aluminum salts" @default.
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• W2022209862 doi "https://doi.org/10.1016/s0304-3940(99)00307-9" @default.
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