MOLECULAR DYNAMICS STUDY OF CYTOCHROME C – LIPID COMPLEXES
Journal: East European Journal of Physics (Vol.4, No. 3)Publication Date: 2017-10-20
Authors : V. Trusova; G. Gorbenko; U. Tarabara; K. Vus; O. Ryzhova;
Page : 54-62
Keywords : cytochrome c; protein-lipid interactions; amyloid; molecular dynamics;
Abstract
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.
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