Open AccessSpectral and structural properties of clotting factor proteins under mechanical stress
Author(s) -
Е. Л. Алексахина,
А. С. Парфенов,
D A Priyatkin,
Nadezda Fomina,
И К Томилова
Publication year - 2021
Publication title -
journal of physics. conference series
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.21
H-Index - 85
eISSN - 1742-6596
pISSN - 1742-6588
DOI - 10.1088/1742-6596/2094/2/022044
Subject(s) - fibrinogen , fibrin , crystallinity , biophysics , chemistry , fluorescence , phase transition , in vivo , crystallography , phase (matter) , factor xiii , materials science , biochemistry , organic chemistry , biology , optics , immunology , physics , microbiology and biotechnology , quantum mechanics
The fluorescence data obtained from BODIPY molecular sensors prove the increase of hydrophobicity of blood plasma proteins, fibrinogen, after in vitro and in vivo pressure episodes, which indicates conformational changes in the structure of the fibrinogen due to the phase transition from α-helices to β-sheets in its superspirals. The phase transition in the supramolecular structure of fibrinogen provides greater hydrophobicity of fibrin, intensifying the visible crystallinity of the fibrin clot observed by infrared spectroscopy, scanning electron microscopy and X-ray imaging.