Different conditions of fibrillogenesis cause polymorphism of lysozyme amyloid fibrils

Structural differences of lysozyme amyloid fibrils prepared under different conditions were examined with the use of electron microscopy, CD spectroscopy together with a specially developed approach based on the absorption and fluorescence spectroscopy of solutions of amyloid fibrils with a specific...

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Bibliographic Details
Published in:Journal of molecular structure 2017-07, Vol.1140, p.52-58
Main Authors: Sulatskaya, Anna I., Rodina, Natalia P., Povarova, Olga I., Kuznetsova, Irina M., Turoverov, Konstantin K.
Format: Article
Language:English
Subjects:
Amyloid fibrils
Equilibrium microdialysis
Lysozyme
Polymorphism
Thioflavin T
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Summary:Structural differences of lysozyme amyloid fibrils prepared under different conditions were examined with the use of electron microscopy, CD spectroscopy together with a specially developed approach based on the absorption and fluorescence spectroscopy of solutions of amyloid fibrils with a specific fluorescent probe thioflavin T, prepared by equilibrium microdialysis. It was shown that the amyloid fibrils differ in their photophysical properties, morphology, parameters of thioflavin T binding. Furthermore, characteristic of the dye bound to fibrils obtained in various conditions are different. These results lead us to conclude that the conditions of fibrillogenesis can influence the rate of formation as well as the properties and structure of investigated amyloid fibrils. [Display omitted] •Lysozyme amyloid fibrils prepared under different conditions were compared.•Fibrillogenesis was visualized by EM and probed by thioflavin T (ThT) fluorescence.•Equilibrium microdialysis was used for ThT-fibrils binding parameters determination.•Fibrils differ in photophysical properties, morphology, parameters of ThT binding.•Influence of fibrillogenesis conditions on polymorphism of fibrils was proved.
ISSN:0022-2860
1872-8014
DOI:10.1016/j.molstruc.2016.10.037