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Amyloid-like fibrils formed from intrinsically disordered caseins: physicochemical and nanomechanical properties
Pan, Kang ; Zhong, Qixin
Soft matter, 2015-08, Vol.11 (29), p.5898-5904
[Periódico revisado por pares]
England
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Título:
Amyloid-like fibrils formed from intrinsically disordered caseins: physicochemical and nanomechanical properties
Autor:
Pan, Kang
;
Zhong, Qixin
Assuntos:
Acids - chemistry
;
Amyloid - chemistry
;
Amyloid - metabolism
;
Atomic structure
;
Caseins - chemistry
;
Caseins - metabolism
;
Dispersions
;
Elastic Modulus
;
Fibrillation
;
Heating
;
Hydrogen-Ion Concentration
;
Hydrolysis
;
Kinetics
;
Lactoglobulins - chemistry
;
Microscopy, Atomic Force
;
Modulus of elasticity
;
Nanostructure
;
Nanostructures - chemistry
;
Protein Structure, Secondary
;
Proteins
;
Rheology
;
Spectroscopy, Fourier Transform Infrared
É parte de:
Soft matter, 2015-08, Vol.11 (29), p.5898-5904
Notas:
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição:
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.
Editor:
England
Idioma:
Inglês
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