Amyloid fibrils from readily available sources: Milk casein and lens crystallin proteins

Heath Ecroyd, Megan Garvey, David C. Thorn, Juliet A. Gerrard, John A. Carver*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

5 Citations (Scopus)

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.

Original languageEnglish
Title of host publicationProtein Nanotechnology
Subtitle of host publicationProtocols, Instrumentation, and Applications, Second Edition
PublisherHumana Press Inc.
Pages103-117
Number of pages15
ISBN (Print)9781627033534
DOIs
Publication statusPublished - 2013
Externally publishedYes

Publication series

NameMethods in Molecular Biology
Volume996
ISSN (Print)1064-3745

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