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

Authors

DOI:

https://doi.org/10.26565/2312-4334-2017-4-04

Keywords:

amyloid fibrils, Thioflavin T, molecular docking, molecular dynamics, fibril twisting

Abstract

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.

Author Biography

  • V. M. Trusova, Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University4 Svobody Sq., Kharkiv, 61022, Ukraine

     

     

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Published

2017-12-15

Issue

Vol. 4 No. 4 (2017): East European Journal of Physics

Section

Original Papers

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How to Cite

THIOFLAVIN T BINDING TO THE MODEL FIBRILS OF LYSOZYME: THE EFFECTS OF FIBRIL TWISTING. (2017). East European Journal of Physics, 4(4), 30-36. https://doi.org/10.26565/2312-4334-2017-4-04