Journal
JOURNAL OF MOLECULAR STRUCTURE
Volume 1140, Issue -, Pages 52-58Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molstruc.2016.10.037
Keywords
Lysozyme; Amyloid fibrils; Polymorphism; Thioflavin T; Equilibrium microdialysis
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Funding
- Russian Foundation of Basic Research [16-54-00230-Bel, 16-04-01614]
- RF President Fellowship [SP-1982.2015.4]
- Molecular and Cell Biology Program of the Russian Academy of Sciences
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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. (C) 2016 Elsevier B.V. All rights reserved.
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