Protein-protein interactions in amyloid deposits

Grant number: DP0449510

Abstract

The aggregation of specific proteins to form insoluble amyloid fibrils is characteristic of several age-related diseases such as type-II diabetes, Alzheimer's disease and Parkinson's disease. In vivo amyloid deposits also contain three prominent non-fibrillar protein components, namely serum amyloid P component, apolipoprotein E and alpha1-antichymotrypsin. These non-fibrillar amyloid components bind to a wide variety of amyloid fibrils, irrespective of the nature of the protein constituent. This proposal is to identify the structural basis for this recognition process, the capacity of non-fibrillar components to cross-link amyloid fibrils to form networks and the influence of these interact..

View full description

Related publications (6)

Scholarly works icon

Thioflavin T fluorescence in human serum: Correlations with vascular health and cardiovascular risk factors

Michael DW Griffin, Leanne M Wilson, Yee-Foong Mok, Andrzej S Januszewski, Andrew M Wilson, Connie S Karschimkus, Evange Romas, Allan B Lee, Tim Godfrey, Melinda Wong, Laurence Clemens, Alicia J Jenkins, Geoffrey J Howlett

2010-02-01

OBJECTIVES: Amyloid fibrils and amyloid-like structures are implicated in atherosclerosis via macrophage activation and inflammati..

Scholarly works icon

Fluorescence Detection of a Lipid-induced Tetrameric Intermediate in Amyloid Fibril Formation by Apolipoprotein C-II

Timothy M Ryan, Geoffrey J Howlett, Michael F Bailey

2008-12-12

The misfolding and self-assembly of proteins into amyloid fibrils that occurs in several debilitating and age-related diseases is ..

Scholarly works icon

Apolipoprotein C-II amyloid fibrils assemble via a reversible pathway that includes fibril breaking and rejoining

Katrina J Binger, Chi LL Pham, Leanne M Wilson, Michael F Bailey, Lynne J Lawrence, Peter Schuck, Geoffrey J Howlett

2008-02-29

Alzheimer's and several other diseases are characterized by the misfolding and assembly of protein subunits into amyloid fibrils. ..

Scholarly works icon

Phospholipid interaction induces molecular-level polymorphism in apolipoprotein C-II amyloid fibrils via alternative assembly pathways

Michael DW Griffin, Melva LY Mok, Leanne M Wilson, Chi LL Pham, Lynne J Waddington, Matthew A Perugini, Geoffrey J Howlett

2008-01-04

A common feature of many of the most important and prominent amyloid-forming proteins is their ability to bind lipids and lipid co..

Scholarly works icon

A structural core within apolipoprotein C-II amyloid fibrils identified using hydrogen exchange and proteolysis

Leanne M Wilson, Yee-Foong Mok, Katrina J Binger, Michael DW Griffin, Haydyn DT Mertens, Feng Lin, John D Wade, Paul R Gooley, Geoffrey J Howlett

2007-03-09

Plasma apolipoproteins show alpha-helical structure in the lipid-bound state and limited conformational stability in the absence o..

Scholarly works icon

High density lipoproteins bind A beta and apolipoprotein C-II amyloid fibrils

LM Wilson, CLL Pham, AJ Jenkins, JD Wade, AF Hill, MA Perugini, GJ Howlett

2006-04-01

Disease-associated amyloid deposits contain both fibrillar and nonfibrillar components. The majority of these amyloid components o..

University of Melbourne Researchers