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

Soft Matter. 2019-08; 
PanKang,ZhongQ
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Recombinant Proteins … A precast 15% gradient polyacrylamide gel from Bio-Rad Laboratories, Inc. (Hercules, CA) was used in SDS-PAGE. 40 μL of a protein sample was mixed with 200 μL of a SDS-PAGE sample buffer (catalog number MB01015, GenScript Corp., Piscataway, NJ) … Get A Quote

摘要

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 Yo... More

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