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On the binding of complement to solid artificial surfaces in vitro.

Jonas Wetterö1, Agneta Askendal, Torbjörn Bengtsson

  • 1Department of Physics and Measurement Technology, Linköping University, Sweden. jonwe@ifm.liu.se

Biomaterials
|January 17, 2002
PubMed
Summary

Artificial surfaces interacting with blood may not covalently bind complement factor 3 (C3) via nucleophilic groups. Protein elution suggests binding relies more on protein-protein interactions and surface forces.

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Area of Science:

  • Biomaterials Science
  • Immunology
  • Surface Chemistry

Background:

  • Artificial surfaces contacting blood can activate the complement system.
  • A prevailing theory suggests covalent binding between complement factor 3 (C3) and surface nucleophilic groups (amine, hydroxyl).
  • This binding is thought to form amide or ester linkages between C3b and the surface.

Purpose of the Study:

  • To investigate the direct covalent binding of C3 to artificial surfaces.
  • To evaluate the role of nucleophilic surfaces and adsorbed proteins in complement binding.
  • To challenge the prevalent covalent linkage model for C3-surface interactions.

Main Methods:

  • Utilized null-ellipsometry to measure complement C3 surface binding.
  • Tested surfaces with amine (-NH2) and hydroxyl (-OH) groups.

Related Experiment Videos

  • Examined surfaces with covalently bound and spontaneously adsorbed immunoglobulin G (IgG).

    • Main Results:

    • Plasma proteins deposited during complement activation were eluted by sodium dodecyl sulfate.
    • Direct covalent binding between C3 and nucleophilic surfaces was of moderate importance, especially in short incubations.
    • The results indicate that the established covalent linkage model is likely inaccurate.

    Conclusions:

    • Direct covalent binding between C3 and artificial nucleophilic surfaces is less significant than previously believed.
    • Complement C3 interactions with surfaces are likely dominated by associations with other adsorbed proteins.
    • Electrostatic and hydrophobic protein-surface interactions play a more prominent role in C3 binding to artificial materials.