Issue 29, 2015

Amyloid-like fibrils formed from intrinsically disordered caseins: physicochemical and nanomechanical properties

Abstract

Amyloid-like fibrils are studied because of their significance in understanding pathogenesis and creating functional materials. Amyloid-like fibrils have been studied by heating globular proteins at acidic conditions. In the present study, intrinsically disordered α-, β-, and κ-caseins were studied to form amyloid-like fibrils at pH 2.0 and 90 °C. No fibrils were observed for α-caseins, and acid hydrolysis was found to be the rate-limiting step of fibrillation of β- and κ-caseins. An increase of β-sheet structure was observed after fibrillation. Nanomechanic analysis of long amyloid-like fibrils using peak-force quantitative nanomechanical atomic force microscopy showed the lowest and highest Young's modulus for β-casein (2.35 ± 0.29 GPa) and κ-casein (4.14 ± 0.66 GPa), respectively. The dispersion with β-casein fibrils had a viscosity more than 10 and 5 times higher than those of κ-casein and β-lactoglobulin, respectively, at 0.1 s−1 at comparable concentrations. The current findings may assist not only the understanding of amyloid fibril formation but also the development of novel functional materials from disordered proteins.

Graphical abstract: Amyloid-like fibrils formed from intrinsically disordered caseins: physicochemical and nanomechanical properties

Supplementary files

Article information

Article type
Paper
Submitted
30 Apr 2015
Accepted
19 Jun 2015
First published
19 Jun 2015

Soft Matter, 2015,11, 5898-5904

Author version available

Amyloid-like fibrils formed from intrinsically disordered caseins: physicochemical and nanomechanical properties

K. Pan and Q. Zhong, Soft Matter, 2015, 11, 5898 DOI: 10.1039/C5SM01037C

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