| Title | Amyloid fibrils from readily available sources: Milk casein and lens crystallin proteins |
| Publication Type | Book |
| Year of Publication | 2013 |
| Authors | Ecroyd, H., Garvey M., Thorn D.C., Gerrard J.A., and Carver J.A. |
| Series Title | Methods in Molecular Biology |
| Volume | 996 |
| Number of Pages | 103 - 117 |
| ISBN | 10643745 (ISSN); 9781627033534 (ISBN) |
| Keywords | amyloid, Animals, article, biocompatibility, biomimetic material, biosensor, Casein, Caseins, cattle, Chromatography, Gel, Chromatography, Ion Exchange, cow, crystallin, Crystallins, Dithiothreitol, lens protein, Methylation, milk, milk protein, nonhuman, Oxidation-Reduction, priority journal, protein aggregation, Protein Multimerization, Reducing Agents, Solutions |
| 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. © 2013 Springer Science+Business Media, New York. |
| URL | http://www.scopus.com/inward/record.url?eid=2-s2.0-84877148754&partnerID=40&md5=3cedebacc155aff00b203b19c81a5296 |
| DOI | 10.1007/978-1-62703-354-1-6 |
