AURAMINE O AS POTENTIAL AMYLOID MARKER: FLUORESCENCE AND MOLECULAR DOCKING STUDIES

East European Journal of Physics. 2017;4(3):63-70

 

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

K. Vus (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
U. Tarabara (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
K. Semenova (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
V. Viter (Department of Molecular and Medical Biophysics V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
O. Nikitina (Department of Molecular and Medical Biophysics 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)

EDITORIAL INFORMATION

Blind peer review

Editorial Board

Instructions for authors

Time From Submission to Publication: 8 weeks

 

Abstract | Full Text

The applicability of Auramine O to the detection and characterization of lysozyme and serum albumin amyloid fibrils has been assessed using the fluorimetric titration and molecular docking. The parameters of the dye binding to native and fibrillar proteins were estimated in terms of the Langmuir adsorption model. It was found that Auramine O displays the high affinity for amyloid fibrils, being of the same order of magnitude as that of the classical amyloid markers. The dye also showed greater fluorescence response to lysozyme fibrils and lower sensitivity to the native protein, than Thioflavin T. Furthermore, unlike Thioflavin T, Auramine O was able to detect the morphological differences between lysozyme and albumin fibrils due to the shifts in the position of the emission maxima of the fibril-incorporated fluorophore. The molecular docking studies revealed that Auramine O and Thioflavin T form the most stable complexes with the G54_L56/S60_W62 groove of lysozyme fibrils, running parallel to the fibril axis. The results obtained suggest the contribution of both hydrophobic and electrostatic interactions to the stabilization of the dye complexes with amyloid fibrils.