Work

Amyloid fibrils: Abnormal protein assembly

Year: 2008

Type: review

Abstract: Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs and tissues. Amyloid is insoluble and is structurally dominated by beta-sheet structure. Unlike other fibrous proteins it does not commonly have a structural, supportive or motility role but is associated with the pathology seen in a range of diseases known as the amyloidoses. These diseases include Alzheimer's, the spongiform encephalopathies and type II diabetes, all of which are progressive disorders with associated high morbidity and mortality. Not surprisingly, research into the physicochemical properties of amyloid and its formation is currently intensely pursued. In this chapter we will highlight the key scientific findings and discuss how the stability of amyloid fibrils impacts on bionanotechnology.

Source: Prion

DOI: 10.4161/pri.2.3.7488

Authors: Roma N. Rambaran, Louise C. Serpell

Institution: University of Sussex

Language: Spanish

Topic: Alzheimer's disease research and treatments

Subfield: Cellular and Molecular Neuroscience

Field: Neuroscience

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: Wellcome Trust, Alzheimer's Research Trust, Biotechnology and Biological Sciences Research Council