Morphological development of beta(1-40) amyloid fibrils.

Abstract:

:The Alzheimer's disease-related peptide beta(1-40) amyloid self-associates to form fibrils exhibiting a morphology characteristic of amyloidogenic proteins. The mechanism of this fibrillization process has yet to be fully elucidated. In this study we have immobilized the beta(1-40) amyloid to flat gold surfaces using thiol-based self-assembled monolayers. Atomic force microscopy reveals the presence of spherical units of beta(1-40) amyloid immediately following the initiation of fibrillization. Short fibrillar structures, termed nascent fibrils, which appear to be formed by the association of these units are also present at this time point. At later time points extended, branching networks of fibrils are observed. Some fibrils exhibit a more beaded appearance and greater axial periodicity than others. No nascent fibrils are seen to be present. We believe that these data identify an early fibril structure which could act as an intermediate in beta-amyloid fibrillization. The oligomeric units of which these nascent fibrils are comprised are also determined.

journal_name

Exp Neurol

journal_title

Experimental neurology

authors

Blackley HK,Patel N,Davies MC,Roberts CJ,Tendler SJ,Wilkinson MJ,Williams PM

doi

10.1006/exnr.1999.7114

keywords:

subject

Has Abstract

pub_date

1999-08-01 00:00:00

pages

437-43

issue

2

eissn

0014-4886

issn

1090-2430

pii

S0014-4886(99)97114-5

journal_volume

158

pub_type

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