Hierarchy and the Mechanism of Fibril formation in ADan Peptides

Surolia, Ira and Reddy, Bhanuprakash G and Sinha, Sharmistha (2006) Hierarchy and the Mechanism of Fibril formation in ADan Peptides. In: Journal of Neurochemistry, 99 (2). pp. 537-548.

PDF Hierarchy_and_the_mechanism_of_fibril_formation_in_ADan_peptides.pdf Restricted to Registered users only Download (613kB) | Request a copy

Abstract

Familial Danish dementia is a neurodegenerative disease which is a consequence of alterations in the BRI gene. The pathological signatures of the disease are cerebral amyloidolysis, parenchymal protein deposits and neuronal degeneration. Synthetic Danish dementia (ADan) peptides are capable of forming fibrillar assemblies in vitro at pH 4.8. However, the morphology of the aggregates formed depends greatly on the form of the peptides (oxidized or reduced). In addition to long slender assemblies (2–5 nm in diameter and several micrometers in length) we report ring-like or annular masses (8–9 nm in diameter and 1–2 mm in perimeter) in the case of the oxidized form of the peptides. The reduced forms mainly aggregate to produce granular heaps. The biophysical and kinetic characterization of the process of aggregation was carried out using different pectroscopic and imaging techniques. Neurotoxicity assays performed on both the forms reveal that the toxicity bears proportionality with the aggregate size.

Item Type:	Journal Article
Publication:	Journal of Neurochemistry
Publisher:	International Society for Neurochemistry
Additional Information:	Copyright of this article belongs to International Society for Neurochemistry.
Keywords:	Amyloids;Annular aggregation;Danish dementia;Fibrils; Protein aggregation.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	06 Mar 2007
Last Modified:	19 Sep 2010 04:32
URI:	http://eprints.iisc.ac.in/id/eprint/9037

Actions (login required)

View Item