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.
journal_name
Neurosci Lettjournal_title
Neuroscience lettersauthors
Bondy SC,Truong Adoi
10.1016/s0304-3940(99)00307-9keywords:
subject
Has Abstractpub_date
1999-05-21 00:00:00pages
25-8issue
1eissn
0304-3940issn
1872-7972pii
S0304-3940(99)00307-9journal_volume
267pub_type
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journal_title:Neuroscience letters
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journal_title:Neuroscience letters
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journal_title:Neuroscience letters
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journal_title:Neuroscience letters
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journal_title:Neuroscience letters
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journal_title:Neuroscience letters
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journal_title:Neuroscience letters
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更新日期:2009-07-03 00:00:00