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Updated: Jun 1, 2026

Improving 2D and 3D Skin In Vitro Models Using Macromolecular Crowding
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An upper limit for macromolecular crowding effects.

Andrew C Miklos1, Conggang Li, Courtney D Sorrell

  • 1Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA. gary_pielak@unc.edu.

BMC Biophysics
|June 2, 2011
PubMed
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Large synthetic microgels do not significantly alter protein stability or dynamics. The microgels

Area of Science:

  • Biophysics
  • Protein dynamics
  • Macromolecular crowding

Background:

  • Cellular environments contain high macromolecule concentrations, impacting protein properties.
  • Macromolecular crowders vary in size and can occupy over 30% of cellular volume.
  • Protein properties differ in concentrated solutions compared to dilute solutions.

Purpose of the Study:

  • To investigate the effect of large synthetic microgels on protein stability and internal dynamics.
  • To understand how size discrepancy influences macromolecular crowding effects.

Main Methods:

  • Studied a globular protein (~2 nm radius) crowded by synthetic microgels (~300 nm radius).
  • Utilized techniques to assess protein rotational and picosecond-nanosecond (ps-ns) backbone dynamics.

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  • Examined protein stability at high volume occupancy (70%).

    • Main Results:

    • No significant changes observed in protein rotational or ps-ns backbone dynamics.
    • Mild protein stabilization (~0.5 kcal/mol at 37°C, pH 5.4) observed at 70% volume occupancy.
    • Absence of strong crowder-protein interactions indicated by unchanged rotational dynamics.

    Conclusions:

    • Large size difference between protein and microgel crowders minimizes crowding effects.
    • Microgel internal structure provides protein-accessible dilute-like environments.
    • Weakly interacting, large microgels do not significantly impact protein dynamics or stability, representing an upper limit for crowding effects.