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Experimental and Imaging Techniques for Examining Fibrin Clot Structures in Normal and Diseased States
Published on: April 1, 2015
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The Structural-Functional Damage of Fibrinogen Oxidized by Hydrogen Peroxide
L V Yurina1,2,3,4, A D Vasilyeva5, V L Kononenko5
1Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia. lyu.yurina@gmail.com.
Doklady. Biochemistry and Biophysics
|July 8, 2020
Summary
Peroxide oxidation alters fibrinogen’s structure, affecting fibrin network properties. This modification reduces fibrinogen’s resistance to plasmin and impairs its stabilization by factor XIIIa.
Area of Science:
- Biochemistry
- Biophysics
- Materials Science
Background:
- Fibrinogen is a key protein in blood coagulation.
- Oxidative stress can modify protein structure and function.
- Understanding fibrinogen oxidation is crucial for hemostasis research.
Purpose of the Study:
- To investigate the impact of peroxide-induced oxidation on fibrinogen.
- To identify specific oxidation sites and their functional consequences.
- To analyze changes in fibrin network properties and stability.
Main Methods:
- Peroxide-induced oxidation of fibrinogen.
- Analysis of primary structure modifications (amino acid residues).
- Dynamic Light Scattering (DLS) for microrheological characterization.
- Assessment of plasmin hydrolysis and factor XIIIa stabilization.
Main Results:
- Oxidation primarily targeted Methionine (Met), Tryptophan (Trp), and Histidine (His) residues.
- Oxidative modification altered the microrheological properties of the fibrin network.
- Fibrinogen oxidation decreased tolerance to plasmin hydrolysis.
- Factor XIIIa's ability to stabilize fibrin gel was impaired.
Conclusions:
- Peroxide oxidation significantly modifies fibrinogen's primary structure and functional characteristics.
- Altered fibrin network microrheology and reduced stability are key outcomes.
- Oxidized fibrinogen exhibits compromised interactions with plasmin and factor XIIIa, impacting hemostasis.
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