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Study of the interaction between collagen and collagenase molecules by optical methods in the presence of chromium ions

Anna V. Petrova 1, a, Irina A. Sergeeva 2, Anna V. Mitrofanova 3, Galina P. Petrova 4
1 PhD student, 2 Associate Professor, 3 alumnus, 4 Professor

1, 2, 3 Lomonosov Moscow State University, Faculty of Physics, Department of Molecular Processes and Extreme States of Matter. Russia, 119991, Moscow, Lenin Hills, 1, building 2

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Proteins perform a lot of vital functions in living organisms: they serve as a material for building cells, tissues and organs, most hormones, hemoglobin and other compounds [1].
Collagenase is currently used in drugs for the treatment of diseases that result from excessive deposition of collagen protein in some organs, leading to disruption of their normal functioning [2, 3]. The most commonly used bacterial collagenase derived from Clostridium histolyticum CHC (the causative agent of gas gangrene) [4-6]. Since collagen makes up one third of all proteins in the human body, a violation of its synthesis can lead to diseases such as Dupuytren's syndrome, Peyronie's disease, etc. [7, 8]. In such cases, the use of an injectable form of collagenase or preparations based on it can help in the degradation of obstructive collagen [9].
However, there are also such diseases in which collagen fibers begin to be arbitrarily destroyed: osteochondrosis, arthrosis, visual impairment, vascular and skin conditions [10]. Protein degradation can be slowed down by using enzyme inhibitors or protein tanning agents. Chromium plating (or tanning) of collagen has long been used not only in the leather industry, but also to stabilize and strengthen the structure of protein molecules.
The aim of this work is to investigate the interaction between collagen and collagenase molecules in the presence of various activators, inhibitors and tanning agents by fluorescence spectroscopy and dynamic light scattering in buffer solutions. It is necessary to identify and analyze the nature of the interaction as a function of time. The use of calcium, zinc, magnesium and chromium salts in this work is due to the influence on the activity of the enzyme of collagenase and on the structure of collagen fibers [11].
As a result of this work, it was revealed that when calcium and zinc ions are added to buffer solutions of collagen and collagenase, the rate of collagen biodegradation increases 2.4 and 1.3 times, respectively. It was found that when magnesium and EDTA ions are added to buffer solutions of collagen and collagenase, the rate of collagen biodegradation decreases by 2 and 2.6 times, respectively.
Based on the results obtained, it can be concluded that chromium ions of various salts (CrCl3, Cr (NO3)3, Cr(CH3CO2)3) equally affect the process of collagenolysis. Also in the presence of chromium ions in buffer solutions of collagen and collagenase, the rate of protein biodegradation decreases 3.8 times, which indicates the formation of cross-links in the protein and strengthening of the protein structure.

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Anna Petrova
Lomonosov Moscow State University


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