Influence of chromium ions on the collagenolysis process in solutions

Abstract

Collagen is the main component of connective tissue and the most common protein in mammals, making up one third of all proteins, It forms the main part of tendons, ligaments, fascia and is part of bones, cartilage and skin.

For the normal functioning of the body, the presence of enzymes that break down proteins is also necessary. The enzyme that catalyzes the breakdown of collagen is collagenase. The ability of the enzyme to biodegradate this protein makes it possible to use drugs based on it quite effectively in medicine: collagen preparations reduce inflammatory reactions, activate reparative processes and shorten the healing time of wounds.

The purpose of this work is to investigate the interaction of collagen and bacterial collagenase molecules with various trivalent chromium salts, which act as tanning agents, by the method of dynamic light scattering. The choice of the method is due to the fact that it allows real-time monitoring of changes in the optical properties of protein molecules under conditions close to physiological.

As a result of the work:
1) the time dependences of the hydrodynamic radius Rh and the translational diffusion coefficient Dt of collagen molecules in solutions containing salts CrCl3, Cr(CH3COO)3, Cr(NO3)3, as well as the catalyst enzyme collagenase were obtained. According to the results of the measurements, it was revealed that the radius of the protein increases with the addition of chromium salts, and decreases with the addition of collagenase.
2) the time dependences of the hydrodynamic radius Rh in
collagen and collagenase solutions with different concentrations of alkali NaOH are constructed.

Speaker

Alisa Pismennaia
Lomonosov Moscow State University
Russia

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