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Related Experiment Videos

The limiting collagen microfibril. The minimum structure demonstrating native axial periodicity

A Veis, A Miller, S J Leibovich

    Biochimica Et Biophysica Acta
    |January 25, 1979
    PubMed
    Summary

    Researchers grew collagen fibers using rapid dialysis, forming gel networks that exuded water. Stretching these networks yielded highly ordered collagen fibrils, revealing thin filaments approximately 40 A in diameter, consistent with collagen microfibrils.

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    Area of Science:

    • Biochemistry
    • Biophysics
    • Materials Science

    Background:

    • Collagen fibrillogenesis is crucial for tissue structure and function.
    • Understanding the structural organization of collagen at the microscale is essential for biomaterials development.

    Purpose of the Study:

    • To investigate the formation and structural properties of collagen fibers grown in vitro.
    • To characterize the relationship between collagen filament assembly and fibril organization.

    Main Methods:

    • Collagen solutions (acid-soluble or neutral salt-soluble) were dialyzed rapidly in 0.5 M acetic acid to induce gel network formation.
    • Protease inhibitors were used throughout collagen extraction and purification.
    • Gel networks were stretched during drying to form fibrous structures.

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  • Small-angle X-ray diffraction and electron microscopy were employed for structural analysis.

    • Main Results:

    • Rapid dialysis induced rapid length-wise filament growth, forming gel-like networks that readily exuded water.
    • Stretched collagen fibers exhibited high ordering, with up to 20 orders of 670 A meridional periodicity observed via X-ray diffraction.
    • Electron microscopy revealed thin filaments (35-40 A diameter) in unstretched gels, corresponding to postulated collagen microfibrils.
    • No cross-striated fibrils were observed, indicating that the 670 A axial periodicity is achieved within these thin filaments.

    Conclusions:

    • Intermolecular packing consistent with the 670 A axial periodicity occurs within approximately 40 A diameter filaments, identified as collagen microfibrils.
    • The study elucidates the in vitro assembly pathway of collagen into ordered fibrous structures.
    • These findings provide insights into collagen self-assembly relevant to biomaterial design and understanding connective tissue structure.