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Soluble dextran-hemoglobin complex as a potential blood substitute.

S C Tam, J Blumenstein, J T Wong

    Proceedings of the National Academy of Sciences of the United States of America
    |June 1, 1976
    PubMed
    Summary
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    Researchers created soluble dextran-hemoglobin complexes using two methods. These complexes bind oxygen reversibly and show slower kidney excretion in rabbits compared to free hemoglobin.

    Area of Science:

    • Biochemistry
    • Biomaterials Science
    • Pharmacology

    Background:

    • Human hemoglobin (Hb) is a potential oxygen carrier but has a short circulation time and rapid renal clearance.
    • Dextran, a polysaccharide, can be modified to create functionalized materials for bioconjugation.
    • Developing stable and effective hemoglobin-based oxygen carriers (HBOCs) remains a significant challenge in biomedical research.

    Purpose of the Study:

    • To synthesize and characterize soluble dextran-hemoglobin complexes using distinct chemical conjugation methods.
    • To evaluate the oxygen-binding properties of the synthesized dextran-hemoglobin complexes.
    • To assess the pharmacokinetic profile of the dextran-hemoglobin complex in a preclinical animal model.

    Main Methods:

    • Synthesis of dextran-hemoglobin complexes via alkylation (hemoglobin reacting with bromoacetylated dextran) and dialdehyde (hemoglobin reacting with periodate-oxidized dextran) methods.

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  • Characterization of oxygen binding using oxygen-binding curves and determination of P50 values.
  • In vivo pharmacokinetic studies in rabbits, comparing renal excretion and circulation time of the complex versus free hemoglobin.

    • Main Results:

    • Two methods successfully yielded soluble dextran-hemoglobin complexes with yields of approximately 80% (alkylation) and 60% (dialdehyde).
    • Both complexes exhibited reversible oxygen binding, but with a leftward shift in oxygen-binding curves (indicating higher oxygen affinity) compared to free hemoglobin.
    • The dextran-hemoglobin complex produced by the alkylation method demonstrated significantly slower renal excretion and prolonged circulation time in rabbits compared to free hemoglobin.

    Conclusions:

    • Soluble dextran-hemoglobin complexes can be effectively synthesized using both alkylation and dialdehyde conjugation strategies.
    • These modified hemoglobin complexes retain reversible oxygen-binding capacity, albeit with altered oxygen affinity.
    • Dextran conjugation significantly improves the pharmacokinetic profile of hemoglobin, reducing renal clearance and extending circulation time, suggesting potential for improved HBOCs.