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Ozone-induced oxidative modification of fibrinogen molecules
M A Rosenfeld1, A N Shchegolikhin, A V Bychkova
1Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334, Russia. markrosenfeld@rambler.ru.
Biochemistry. Biokhimiia
|November 19, 2013
Summary
Ozone oxidation alters fibrinogen structure, affecting fibrin gel formation and protein fragments. This study details the molecular changes and their impact on fibrinogen
Area of Science:
- Biochemistry
- Protein Chemistry
- Oxidative Stress
Background:
- Fibrinogen is crucial for blood clot formation.
- Oxidative damage can alter protein structure and function.
- Understanding ozone's effect on fibrinogen is important for various biological and medical contexts.
Purpose of the Study:
- To investigate the molecular mechanisms of ozone-induced oxidation in fibrinogen.
- To analyze the impact of oxidation on fibrinogen's conversion to fibrin and the resulting gel properties.
- To characterize the structural and dynamical changes in fibrinogen and its fragments upon oxidation.
Main Methods:
- Infrared (IR) spectroscopy to analyze functional group transformations.
- Electron Paramagnetic Resonance (EPR) spectroscopy to assess structural and dynamical modifications.
- Enzymatic conversion of oxidized fibrinogen to fibrin using thrombin and ancistron.
Main Results:
- Ozone oxidation of fibrinogen leads to altered fibrin gel characteristics (higher weight/length ratio).
- IR spectroscopy revealed significant changes in functional groups (N-H, C-H bonds) and specific amino acid residues (methionine, tryptophan, histidine, phenylalanine) in D and E fragments.
- Fragment D showed greater sensitivity to ozone oxidation than fragment E.
- EPR spectroscopy indicated structural and dynamical modifications in the D and E fragments due to oxidation.
Conclusions:
- Ozone oxidation significantly modifies fibrinogen's molecular structure, impacting its functional properties.
- Fibrinogen fragment D is more susceptible to oxidative damage than fragment E.
- The observed changes in fibrinogen structure and dynamics are linked to its three-dimensional conformation and susceptibility to ozone.
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