Potentiation of beta-folding of beta-amyloid peptide 25-35 by aluminum salts.

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 Lett

journal_title

Neuroscience letters

authors

Bondy SC,Truong A

doi

10.1016/s0304-3940(99)00307-9

keywords:

subject

Has Abstract

pub_date

1999-05-21 00:00:00

pages

25-8

issue

1

eissn

0304-3940

issn

1872-7972

pii

S0304-3940(99)00307-9

journal_volume

267

pub_type

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