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Monomer diffusion into polymer domains in sickle hemoglobin.

M R Cho1, F A Ferrone

  • 1Department of Physics and Atmospheric Science, Drexel University, Philadelphia, Pennsylvania 19104.

Biophysical Journal
|October 1, 1990
PubMed
Summary

Sickle hemoglobin gelation involves polymer domain formation. Monomer diffusion into these domains significantly increases hemoglobin concentration, a process consistent with a simple diffusion model.

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Area of Science:

  • Biophysics
  • Hematology
  • Polymer Science

Background:

  • Sickle cell disease is characterized by the gelation of sickle hemoglobin (HbS).
  • This gelation involves the formation of ordered polymer structures within red blood cells.
  • Understanding the kinetics and mechanisms of HbS polymerization is crucial for therapeutic development.

Purpose of the Study:

  • To investigate the mechanism of monomer diffusion into forming sickle hemoglobin polymer domains.
  • To quantify the rate and extent of hemoglobin concentration increase within these domains.
  • To assess the influence of temperature on the diffusion process.

Main Methods:

  • In situ observation of polymer domain formation using microscopy.
  • Analysis of monomer diffusion kinetics into developing polymer domains.

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  • Comparison of experimental concentration data with theoretical models.

    • Main Results:

    • Observed diffusion of monomers into polymer domains, leading to increased total hemoglobin concentration.
    • Maximum attained concentrations within domains are comparable to pellet concentrations from sedimentation experiments (0.5-0.55 g/cm³).
    • The half-time for monomer diffusion into 25-micron radius domains is approximately 50 seconds and shows weak temperature dependence.

    Conclusions:

    • Monomer diffusion into sickle hemoglobin polymer domains is a significant factor in their growth and internal concentration.
    • The observed diffusion kinetics and weak temperature dependence support a simple diffusion model for this process.
    • These findings provide insights into the physical mechanisms underlying sickle hemoglobin gelation.