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Fibrin aggregation before sol-gel transition

P Wiltzius, G Dietler, W Känzig

    Biophysical Journal
    |May 1, 1982
    PubMed
    Summary
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    Fibrinogen polymerization was studied using light scattering. Monomeric units of 75-nm length aggregate end-to-end and in staggered patterns, with fibrinopeptide A release being crucial for this process.

    Area of Science:

    • Biophysics
    • Polymer Science
    • Biochemistry

    Background:

    • Fibrinogen is a key protein in blood coagulation.
    • Understanding fibrinogen polymerization is crucial for hemostasis and thrombosis research.
    • The process involves the release of fibrinopeptides and subsequent aggregation.

    Purpose of the Study:

    • To investigate the aggregation pathways of fibrinogen during polymerization.
    • To compare the effects of thrombin and reptilase on fibrinogen polymerization kinetics.
    • To validate aggregation models using light scattering data.

    Main Methods:

    • Static and dynamic light scattering were used to monitor fibrinogen polymerization over several hours.
    • Fibrinogen solutions were incubated with small quantities of reptilase or thrombin.

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  • Experimental data were compared with model calculations based on the Flory-Stockmayer distribution.

    • Main Results:

    • Fibrinogen monomers (75-nm length) were observed to aggregate.
    • Early aggregation (0 ≤ λ ≤ 0.3) occurred end-to-end.
    • Later aggregation (0.3 ≤ λ < 1) showed a staggered overlap pattern.
    • No significant difference in aggregation was observed between thrombin and reptilase activation before the gel point.

    Conclusions:

    • The release of fibrinopeptides A is essential for initiating fibrinogen aggregation.
    • The aggregation mechanism transitions from end-to-end to staggered overlap as polymerization progresses.
    • The Flory-Stockmayer model accurately describes the sol-gel phase transition in fibrinogen polymerization.