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Surface Plasmon Resonance for the Analysis of β-Amyloid Interactions and Fibril Formation in Alzheimer's Disease Research


Aguilar, MI and Small, DH, Surface Plasmon Resonance for the Analysis of β-Amyloid Interactions and Fibril Formation in Alzheimer's Disease Research, Neurotoxicity Research: An International Journal on Processes and Mechanisms in Neurodegeneration, Apoptosis, Neuroprotection and Regeneration, 7, (1-2) pp. 17-27. ISSN 1029-8428 (2005) [Refereed Article]

DOI: doi:10.1007/BF03033773


Alzheimer's disease (AD) is a neurodegenerative disorder characterised by the accumulation of amyloid deposits, the major component of which is a 4 kDa polypeptide known as -amyloid protein (A). Identifying the mechanism underlying the formation of A and the pathways that lead to its toxicity is crucial to understanding the mechanism of AD and addressing the urgent need for new and effective treatments for AD. The accumulation of A is the result of a complex interplay between genetic and environmental factors that affect the generation, clearance and aggregation of the peptide. Because of its propensity to aggregate, A builds up in the brain and assembles into amyloid fibrils, ultimately creating amyloid plaques (APs) and cerebral amyloid angiopathy (CAA). A has been shown to interact with a number of intracellular and extracellular molecules, but the relative contribution of these interactions to the toxicity of A is not well understood. A critical step in characterising the importance of these interactions is the ability to measure both the affinity and kinetics of these interactions. Surface plasmon resonance (SPR) spectroscopy has become a widely used technique to study molecular interactions such as antibody-antigen, DNA-DNA, DNA-protein, protein-protein, receptor-ligand and peptide- and protein-membrane interactions. This article reviews the application of SPR to the study of the molecular interactions associated with AD and how this information enhances our molecular understanding of A-mediated toxicity

Item Details

Item Type:Refereed Article
Research Division:Biomedical and Clinical Sciences
Research Group:Neurosciences
Research Field:Neurosciences not elsewhere classified
Objective Division:Health
Objective Group:Clinical health
Objective Field:Clinical health not elsewhere classified
UTAS Author:Small, DH (Professor David Small)
ID Code:61373
Year Published:2005
Web of Science® Times Cited:43
Deposited By:Menzies Institute for Medical Research
Deposited On:2010-03-03
Last Modified:2010-09-16

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