NOVEL CYANINE DYES AS POTENTIAL AMYLOID PROBES: A FLUORESCENCE STUDY

East European Journal of Physics. 2018;5(1):41-46

 

Journal Homepage

Journal Title: East European Journal of Physics

ISSN: 2312-4334 (Print); 2312-4539 (Online)

Publisher: V.N. Karazin Kharkiv National University Publishing

Society/Institution: V.N. Karazin Kharkiv National University

LCC Subject Category: Science: Physics

Country of publisher: Ukraine

Language of fulltext: Russian, Ukrainian, English

Full-text formats available: PDF

 

AUTHORS

U. Tarabara (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
K. Vus (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
A. Kurutos (Faculty of Chemistry and Pharmacy, Sofia University, ‘‘St. Kliment Ohridski’’, 1 blv. J. Bourchier, Sofia, 1164, Bulgaria)
O. Ryzhova (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
V. Trusova (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
G. Gorbenko (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
N. Gadjev (Faculty of Chemistry and Pharmacy, Sofia University, ‘‘St. Kliment Ohridski’’, 1 blv. J. Bourchier, Sofia, 1164, Bulgaria)
T. Deligeorgiev (Faculty of Chemistry and Pharmacy, Sofia University, ‘‘St. Kliment Ohridski’’, 1 blv. J. Bourchier, Sofia, 1164, Bulgaria)

EDITORIAL INFORMATION

Blind peer review

Editorial Board

Instructions for authors

Time From Submission to Publication: 8 weeks

 

Abstract | Full Text

The applicability of the novel heptamethine cyanine dyes AK7-5 and AK7-6 to the detection and characterization of one-dimensional protein aggregates (amyloid fibrils) associated with numerous pathologies has been evaluated using the method of fluorescence spectroscopy. It was found that both the monomeric and aggregated forms of these dyes can bind to amyloidogenic protein lysozyme, but the concomitant changes in the electronic structure of H-aggregates render them capable of fluorescing. The growth of the hypsochromic bands with negligible changes of the monomeric peaks induced by the native protein and the opposite effects induced by the lysozyme fibrils suggest that the native lysozyme has more binding sites for the dye aggregates than fibrillar protein, while the fibril grooves represent specific binding site for the dyes monomers. The observed spectral behavior of the cyanine dyes, viz. significant distinctions in the fluorescence responses produced by the monomeric and fibrillar forms of lysozyme, suggest the possibility of recruiting these compounds as fluorescent amyloid markers along with the classical amyloid marker Thioflavin T.