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Plasma protein adsorption: the big twelve.

J D Andrade1, V Hlady

  • 1Department of Bioengineering, University of Utah, Salt Lake City 84112.

Annals of the New York Academy of Sciences
|January 1, 1987
PubMed
Summary

Understanding protein adsorption at interfaces requires considering factors like mass transport and protein structure. Lipoproteins may dominate adsorption on certain surfaces due to their unique properties.

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Area of Science:

  • Surface Chemistry
  • Biomaterials Science
  • Physical Chemistry

Background:

  • Protein adsorption at solid-liquid interfaces is crucial in various scientific and technological fields.
  • Understanding the adsorption behavior of plasma proteins is essential for biomedical applications.
  • Existing models often simplify the complex interactions governing protein adsorption.

Purpose of the Study:

  • To discuss general principles of protein adsorption at solid-liquid interfaces.
  • To survey major plasma protein components and their adsorption characteristics.
  • To explore factors influencing protein adsorption, including structure, concentration, and surface properties.

Main Methods:

  • Qualitative kinetic modeling incorporating mass transport, interaction energies, and conformational changes.
  • Survey of "The Big Twelve" plasma proteins (concentration > 1 mg/mL).
  • Analysis of protein size, concentration, diffusion coefficients, structure, function, and surface denaturability.

Main Results:

  • Protein adsorption is influenced by mass transport, initial energies, surface-induced conformational changes, and desorption.
  • Lipoproteins may dominate adsorption on mobile elastomeric polymer surfaces due to their thermal properties.
  • Carbohydrate moieties on proteins might affect their adsorption behavior.

Conclusions:

  • A comprehensive understanding of protein adsorption necessitates detailed consideration of individual protein structures and characteristics.
  • Thorough characterization of both the solid surface and the protein/aqueous environment is critical.
  • Further research into specific protein-surface interactions is required for accurate modeling and prediction.

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