THIOFLAVIN T BINDING TO THE MODEL FIBRILS OF LYSOZYME: THE EFFECTS OF FIBRIL TWISTING

East European Journal of Physics. 2017;4(4):30-36

 

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

A. E. Kokorev (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
V. M. Trusova (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
K. O. Vus (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
U. K. Tarabara (Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, Ukraine)
G. P. 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

Amyloid fibrils are highly ordered insoluble protein aggregates that are involved in molecular etiology of a number of severe disorders, including Alzheimer's, Parkinson’s and prion’s diseases, some types of systemic amyloidosis, etc. One of the most effective approaches to detecting the amyloid fibrils is based on monitoring the spectral behavior of specific fluorescent dye Thioflavin T (ThT). Using the molecular docking and molecular dynamics tools, such as PatchDock, FireDock, CreateFibril and GROMACS, the model of twisted K-peptide fibril that supposedly represent the core region of lysozyme amyloid fibrils, has been constructed and analyzed. The effect of fibril twisting angle on the binding characteristics of ThT has been evaluated. The results obtained strongly suggest that ThT specificity for the twisted ribbon fibril polymorphs is primarily determined by the curvature effects rather than amino acid composition of fibril grooveswhich accomodate ThT molecule.