Study of the Mechanism of Interaction of Ficin with a Graft Copolymer of Carboxymethyl Cellulose Sodium Salt and N-vinylimidazole Using Molecular Docking, as Well as Infrared and Raman Spectroscopy.

Autor: Sorokin, A. V., Goncharova, S. S., Lavlinskaya, M. S., Holyavka, M. G., Zuev, Yu. F., Faizullin, D. A., Kondtatyev, M. S., Artyukhov, V. G.
Zdroj: Biophysics; Apr2023, Vol. 68 Issue 2, p182-189, 8p
Abstrakt: The mechanism of interaction of ficin with a graft copolymer of the sodium salt of carboxymethylcellulose and N-vinylimidazole has been investigated by methods of flexible molecular docking, infrared and Raman spectroscopy. Functional groups and fragments of graft copolymer molecules, as well as amino-acid residues forming the primary structure of the enzyme that interacts between the ficin and the graft copolymer, have been identified. It was shown that Raman spectroscopy gives more complete representation of fragments of graft copolymer macromolecules interacting with protein compared to infrared spectroscopy. It has been found that the amino-acid residues forming the active site of ficin were involved in the formation of hydrogen bonds and hydrophobic interactions with the graft copolymer, which led to an increase in the proteolytic activity of the conjugated enzyme. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
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