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Protofibrils within fibrin fibres are packed together in a regular array
Giulio Caracciolo1, Marco De Spirito, Agostina Congiu Castellano
1Dept of Biochemical Sciences, University of Rome La Sapienza, Piazzale Aldo Moro 5, I-00185 Rome, Italy.
Thrombosis and Haemostasis
|April 2, 2003
Summary
Energy Dispersive X-ray Diffraction reveals fibrin fibres exhibit ordered protofibril arrangements. This confirms a crystalline packing structure in fibrin, supporting the multibundle model.
Area of Science:
- Biophysics
- Materials Science
- Biochemistry
Background:
- Fibrin fibres are crucial for blood clot formation.
- Understanding fibrin's internal structure is key to comprehending its mechanical properties.
- Previous models proposed different arrangements of protofibrils within fibrin fibres.
Purpose of the Study:
- To investigate the inner structure of fibrin fibres.
- To determine the arrangement and order of protofibrils within fibrin fibres.
- To validate existing models of fibrin fibre structure.
Main Methods:
- Fibrin fibres were grown from fibrinogen solution activated by human alpha-thrombin.
- Energy Dispersive X-ray Diffraction (EDXRD) was employed to analyze the fibre structure.
- Experiments were conducted on unperturbed wet samples to preserve native structure.
Main Results:
- A characteristic 22.5 nm repeat distance was observed, indicating high longitudinal order of protofibrils.
- A significant peak at 18.1 nm (and its second-order reflection) demonstrated high lateral order.
- The diffraction patterns confirmed crystalline axial and equatorial packing of protofibrils.
Conclusions:
- The findings provide direct experimental evidence for the close association of protofibrils.
- The results support the multibundle model of fibrin fibre structure.
- The study confirms a high degree of both longitudinal and lateral order in fibrin fibres.