Investigation of the effect of transition metals (MN, CO, GD) on the spatial structure of fibrinopeptide B by NMR spectroscopy

Publication date: 15 March 2020Source: Journal of Molecular Structure, Volume 1204Author(s): Adeliia R. Faizullina, Dmitriy S. Blokhin, Aleksandra M. Kusova, Vladimir V. KlochkovAbstractFibrinopeptide B (GluFib) is one of the factors of thrombosis. Normal soluble blood protein, fibrinogen (fibrinopeptide A and fibrinopeptide B), is transformed into the insoluble fibrin, which in the form of filaments adheres to the vessel wall at the site of injury, forming a grid. In the literature, it is noted that a violation of blood coagulation under the influence of cobalt and lanthanides compounds has been established. It is possible that the reason is the change in the structure of the molecules of fibrin fibers under the influence of cobalt and lanthanides influences. In this paper the spatial structure of GluFib was investigated with manganese (II) chloride, cobalt (II) chloride and gadolinium (III) chloride by NMR spectroscopy. The spatial structures were obtained by applying 1D and 2D 1H–1H NMR spectroscopy (TOCSY, ROESY). The chemical shifts of some 1H NMR signals of GluFib in complex with cobalt and gadolinium salts have changed. The changing chemical shifts belong to betta-group atoms of 7 and 8 glutamic acid. Analyzing spectra, it was found that ions of cobalt and gadolinium interact with GluFib, integrating between the amino acid residues of the seventh and eighth glutamic acids. Manganese ions don’t interact with fibrinopeptide B molecule. In our work we were received th...
Source: Journal of Molecular Structure - Category: Molecular Biology Source Type: research