Thioflavin t behavior in lysozyme - lipid systems

  • G. P. Gorbenko V.N. Karazin Kharkov National University
  • V. M. Ioffe V.N. Karazin Kharkov National University
  • P. K.J. Kinnunen Institute of Biomedicine, University of Helsinki
Keywords: amyloid fibrils, thioflavin T, liposomes, lysozyme

Abstract

The applicability of thioflavin T (ThT) to the detection of amyloid-like aggregates formed in the membrane environment was evaluated using a lysozyme-lipid model system. It was found that ThT is capable of partitioning into lipid bilayers composed of zwitterionic (1- palmitoyl -2-oleoyl-sn-glycerol-3-phosphocholine (POPC)) and anionic (1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphoglycerol (POPG)) phospholipids. The ability of ThT to associate non-specifically with lysozyme in its native state was uncovered. These properties of ThT may impose limits on the use of this dye for the identification of membrane-induced fibrillar structures.

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Author Biographies

G. P. Gorbenko, V.N. Karazin Kharkov National University

4 Svobody Sq., Kharkov, 61077, Ukraine

V. M. Ioffe, V.N. Karazin Kharkov National University

4 Svobody Sq., Kharkov, 61077, Ukraine

P. K.J. Kinnunen, Institute of Biomedicine, University of Helsinki

Haartmaninkatu, 8FIN-00014, Finland

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Published
2005-06-06
Cited
How to Cite
Gorbenko, G. P., Ioffe, V. M., & Kinnunen, P. K. (2005). Thioflavin t behavior in lysozyme - lipid systems. Biophysical Bulletin, 2(16), 30-32. Retrieved from https://periodicals.karazin.ua/biophysvisnyk/article/view/13328

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