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Models of fibrin.

J Hermans

    Proceedings of the National Academy of Sciences of the United States of America
    |March 1, 1979
    PubMed
    Summary
    This summary is machine-generated.

    New models of fibrin fibers explain their high specific volume. These models feature helical protofibrils with specific monomer arrangements and packing symmetries, crucial for understanding fibrin structure and function.

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    Area of Science:

    • Biophysics
    • Structural Biology
    • Materials Science

    Background:

    • Fibrin fibers are key components of blood clots.
    • Their high specific volume is an experimentally observed property.
    • Understanding fibrin structure is crucial for thrombosis and hemostasis research.

    Purpose of the Study:

    • To propose high-symmetry models of fibrin fibers.
    • To explain the experimentally observed high specific volume of fibrin fibers.
    • To investigate the structural basis for fibrin's mechanical properties.

    Main Methods:

    • Development of theoretical models based on fibrin monomer structure (three-domain Hall and Slayter).
    • Modeling of protofibril formation with half-overlapping monomers.
    • Analysis of helical arrangements and packing symmetries (space groups) of protofibrils.

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  • Investigating monomer displacement (lateral shift or tilt) and its effect on D-domain positioning.

    • Main Results:

    • Proposed models successfully reproduce the high specific volume of fibrin fibers.
    • Models incorporate helical protofibrils with monomers arranged in parallel to the fiber axis.
    • Achieving high specific volume requires displacement of D-domains from protofibril helical axes.
    • Tilted monomers lead to more interconnected fibers compared to laterally shifted or nontilted monomers.

    Conclusions:

    • The proposed high-symmetry models provide a structural basis for the high specific volume of fibrin fibers.
    • Monomer tilt is a critical factor for enhanced lateral connectivity and fiber stability.
    • These findings advance our understanding of fibrin polymerization and fiber assembly.