Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/78432
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Type: Book chapter
Title: Amyloid fibrils from readily available sources: Milk casein and lens crystallin proteins
Author: Ecroyd, H.
Garvey, M.
Thorn, D.
Gerrard, J.
Carver, J.
Citation: Protein nanotechnology : protocols, instrumentation, and applications, 2013 / Vo Dinh, T. (ed./s), vol.996, pp.103-117
Publisher: Springer
Publisher Place: United States
Issue Date: 2013
ISBN: 9781627033534
Editor: Vo Dinh, T.
Statement of
Responsibility: 
Heath Ecroyd, Megan Garvey, David C. Thorn, Juliet A. Gerrard, and John A. Carver
Abstract: Amyloid fibrils are a highly ordered and robust aggregated form of protein structure in which the protein components are arranged in long fibrillar arrays comprised of β-sheet. Because of these properties, along with their biocompatibility, amyloid fibrils have attracted much research attention as bionanomaterials, for example as template structures (in some cases following modification) that can be used as biosensors, encapsulators, and biomimetic materials. To use amyloid fibrils for such a range of applications will require them to be obtained relatively easily in large quantities. In this chapter, we describe methods for isolating crystallin and casein proteins from readily available sources that contain abundant protein, i.e., the eye lens and milk, respectively, and the subsequent conversion of these proteins into amyloid fibrils.
Keywords: Crystallins
Small heat-shock proteins
Caseins
Amyloid fibrils
Bionanomaterials
Lens proteins
Milk proteins
Protein aggregation
Rights: © Springer Science+Business Media New York 2013
DOI: 10.1007/978-1-62703-354-1_6
Appears in Collections:Aurora harvest 4
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