Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry

Area of Science:

• Biochemistry
• Materials Science
• Protein Chemistry

Background:

• Fibrinogen is a key protein in blood coagulation.
• Oxidative stress can alter protein structure and function.
• Understanding fibrinogen's response to oxidation is crucial for studying thrombosis and related diseases.

Purpose of the Study:

• To investigate the thermal denaturation of fibrinogen under induced oxidation for the first time.
• To characterize structural changes in fibrinogen upon oxidation using differential scanning calorimetry.

Main Methods:

• Differential scanning calorimetry (DSC) was employed to study thermal denaturation.
• Induced oxidation was applied to fibrinogen samples.
• Analysis of denaturation temperature, denaturation enthalpy, and van't Hoff enthalpy.

Main Results:

• All detected fibrinogen structural elements (D region, αC-domain, and E region) are susceptible to oxidation.
• Oxidation induced measurable changes in the thermal denaturation profiles of fibrinogen.
• Specific parameters like denaturation temperature and enthalpy were altered by oxidation.

Conclusions:

• Oxidation significantly impacts the structural integrity and thermal stability of fibrinogen.
• DSC is a valuable tool for detecting oxidation-induced structural modifications in fibrinogen.
• These findings contribute to understanding fibrinogen's role in oxidative stress-related conditions.