Amyloid formation via supramolecular peptide assemblies.

Abstract:

:Amyloid fibrils have been classically defined as linear, nonbranched polymeric proteins with a cross beta-sheet structure and the ability to alter the optical properties of the amyloid-specific dye Congo Red. Mounting evidence suggests that soluble oligomeric peptide assemblies approximately 2-20 nm in diameter are critical intermediates in amyloid formation. Using a pathogenic prion protein peptide comprised of residues 23-144, we demonstrate that, under quiescent but not agitated conditions, much larger globular assemblies up to 1 mum in diameter are made. These globules precede fibril formation and directly interact with growing fibril bundles. Fibrils made via these large spherical peptide assemblies displayed a remarkable diversity of ultrastructural features. Fibrillization of the Abeta1-40 peptide under similar conditions yielded similar results, suggesting a mechanism of general amyloid formation that can proceed through intermediates much larger than those previously described. Our data suggest that simply changing the physical microenvironment can profoundly influence the mechanism of amyloid formation and yield fibrils with novel ultrastructural properties.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Moore RA,Hayes SF,Fischer ER,Priola SA

doi

10.1021/bi700247y

subject

Has Abstract

pub_date

2007-06-19 00:00:00

pages

7079-87

issue

24

eissn

0006-2960

issn

1520-4995

journal_volume

46

pub_type

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