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Changes in adsorbed fibrinogen upon conversion to fibrin.
Kenyon M Evans-Nguyen1, Ryan R Fuierer, Brian D Fitchett
1Department of Chemistry, University of North Carolina at Chapel Hill, North Carolina 27599, USA.
Langmuir : the ACS Journal of Surfaces and Colloids
|May 17, 2006
Summary
Thrombin converts adsorbed fibrinogen to fibrin, causing mass loss and a more compact layer. This conversion significantly alters fibrinogen conformation beyond simple peptide cleavage.
Area of Science:
- Biochemistry
- Surface Science
- Biomaterials
Background:
- Fibrinogen is a key protein in blood coagulation.
- Thrombin is the enzyme responsible for converting fibrinogen to fibrin.
- Understanding the conversion process at surfaces is crucial for biomaterial applications.
Purpose of the Study:
- To investigate the structural and binding changes of adsorbed fibrinogen upon conversion to fibrin.
- To characterize the conformational alterations induced by thrombin-catalyzed fibrinopeptide release.
Main Methods:
- Surface Plasmon Resonance (SPR) for mass and elutability measurements.
- Quartz Crystal Microbalance (QCM) for acoustic mass monitoring.
- Atomic Force Microscopy (AFM) for surface height and morphology analysis.
- Sum Frequency Generation (SFG) and elutability assays were also employed.
Main Results:
- Thrombin exposure led to mass loss, indicating fibrinopeptide release and fibrin formation.
- The adsorbed fibrin layer became more compact and strongly bound to the surface.
- Elutability by Triton X-100 decreased significantly (90% to 6%).
- AFM revealed a reduction in adsorbed layer height (5.5 nm to 1.7 nm).
Conclusions:
- Thrombin-catalyzed fibrinopeptide release induces substantial conformational changes in fibrinogen.
- The conversion results in a denser, more adherent fibrin layer on the surface.
- These findings provide insights into fibrin formation dynamics at interfaces.