title: Amyloid fibrils: abnormal protein assembly.
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.
authors.affiliation: Department of Chemistry and Biochemistry, School of Life Sciences, University of Sussex, Falmer, UK.
authors.forename: Roma N
authors.initials: RN
authors.lastname: Rambaran
authors.forename: Louise C
authors.initials: LC
authors.lastname: Serpell
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism* / Q000633:toxicity / Q000648:ultrastructure; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D036103:Nanotechnology; D020836:Protein Structure, Quaternary
chemical_list: D000682:Amyloid