Novel Amyloid Fibrillar Networks Derived from a Globular Protein: β-Lactoglobulin
| Autor: | Allan H. Clark, Walraj S Gosal, Paul D. A. Pudney, Simon B. Ross-Murphy |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
chemistry.chemical_classification
Amyloid Globular protein Supramolecular chemistry macromolecular substances Surfaces and Interfaces Condensed Matter Physics Fibril In vitro Turn (biochemistry) Biochemistry chemistry Electrochemistry General Materials Science Protein folding Protein secondary structure Spectroscopy |
| Zdroj: | Langmuir. 18:7174-7181 |
| ISSN: | 1520-5827 0743-7463 |
| DOI: | 10.1021/la025531a |
| Popis: | Biology provides us with a unique set of self-assembled fibrillar networks in the form of amyloid fibrils, derived from the self-assembly of a number of peptides or misfolded proteins. These, in turn, are associated with a number of diseases such as Alzheimer's, Creutzfeldt−Jakob disease (CJD), and type II diabetes. Recently, generating such supramolecular peptidic structures in vitro has led to a class of novel materials. In this multidistance scale, multidisciplinary study, we highlight various regimes whereby fibrils may be engineered by initiating self-assembly through the unfolding of a non-disease- associated globular protein, β-lactoglobulin (Mw ∼ 18 000, 162 residues). In particular, fibrils were generated by traditional thermal methods at pH 2, or, in a novel approach, by incubation in solvent−water mixtures such as water−2,2,2-trifluoroethanol. These treatments lead to fibrils of distinct structure and morphology. Secondary structure analyses of these by Fourier transform infrared spectroscopy (... |
| Databáze: | OpenAIRE |
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