MODELING OF AMYLOID FIBRIL BINDING TO THE LIPID BILAYER

doi:10.26565/2312-4334-2015-2-06

Valeriya Trusova Department of Nuclear and Medical Physics, V.N. Karazin Kharkov National University 4 Svobody Sq., Kharkov, 61022, Ukraine https://orcid.org/0000-0002-7087-071X

DOI: https://doi.org/10.26565/2312-4334-2015-2-06

Abstract

Using the different computational approaches, we constructed the core region of amyloid fibrils from lysozyme, Aβ-protein and apolioprotein A-I, and studied the adsorption of fibrillar aggregates onto lipid bilayer surface. The structures of amyloids differing in their twisting angle were generated with CreateFibril software. The stability of the obtained assemblies was assessed by means of AQUASOL tool, and the twisting angle providing the most stable conformation was identified. The energetically favorable orientation of the fibrils within the lipid membranes was predicted based on PPM server. It was found that increasing amyloid periodicity bring about the rise in free energy of peptide transfer from aqueous to membrane phase.

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Author Biography

Valeriya Trusova, Department of Nuclear and Medical Physics, V.N. Karazin Kharkov National University 4 Svobody Sq., Kharkov, 61022, Ukraine

valtrusova@yahoo.com

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