MOLECULAR DYNAMICS STUDY OF CYTOCHROME C – LIPID COMPLEXES

East European Journal of Physics. 2017;4(3):54-62

 

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: Ukrainian, English, Russian

Full-text formats available: PDF

 

AUTHORS

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)
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)
O. Ryzhova (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 interactions between a mitochondrial hemoprotein cytochrome c (cyt c) and the model lipid membranes composed of zwitterionic lipid phosphatidylcholine (PC) and anionic lipids phosphatidylglycerol (PG), phosphatidylserine (PS) or cardiolipin (CL) were studied using the method of molecular dynamics. It was found that cyt c structure remains virtually unchanged in the protein complexes with PC/PG or PC/PS bilayers. In turn, protein binding to PC/CL bilayer is followed by the rise in cyt c radius of gyration and root-mean-square fluctuations. The magnitude of these changes was demonstrated to increase with the anionic lipid content. The revealed effect was interpreted in terms of the partial unfolding of polypeptide chain in the region Ala15-Leu32, widening of the heme crevice and enhancement of the conformational fluctuations in the region Pro76-Asp93 upon increasing the CL molar fraction from 5 to 25%. The results obtained seem to be of utmost importance in the context of amyloidogenic propensity of cyt c.