Ozone-induced damage of fibrinogen molecules: identification of oxidation sites by high-resolution mass spectrometry.

Ozone-induced damage of fibrinogen molecules: identification of oxidation sites by high-resolution mass spectrometry. Free Radic Res. 2019 Apr 01;:1-651 Authors: Yurina L, Vasilyeva A, Indeykina M, Bugrova A, Biryukova M, Kononikhin A, Nikolaev E, Rosenfeld M Abstract Fibrinogen is highly susceptible to oxidation compared to other plasma proteins. Fibrinogen oxidation damages its structure and affects the protein function. Ozone-induced oxidative modifications of the fibrinogen Aα, Bβ, and γ polypeptide chains upon addition of various amounts of the oxidizer were studied by mass spectrometry. Amino acid residues located on all three chains and main structural parts of the protein were revealed to be involved in oxidation. The αC-connector was shown to be most vulnerable to oxidation as compared to other structural parts while E region turned out to be the most protected area of the protein. For the first time, it was established that numerous amino acid residues responsible for the conversion of fibrinogen to fibrin remain unaffected upon fibrinogen oxidation. The data we have obtained in this study indicate that none of the identified residues, which are considered crucial for the binding of both hole "a" and hole "b" to knob "A" and knob "B", respectively, as well as those responsible for the thrombin binding to fibrinogen E region have been subjected to chemical alterations under moderate oxidation. The data on fibrinogen oxid...
Source: Free Radical Research - Category: Research Tags: Free Radic Res Source Type: research