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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 (M_w ∼ 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 …