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Erythromycin binding to human serum

G A Dette, H Knothe, G Herrmann

    Biochemical Pharmacology
    |March 15, 1982
    PubMed
    Summary
    This summary is machine-generated.

    Erythromycin binds reversibly to human serum proteins at specific, saturable sites. This binding is pH-dependent and characterized by an apparent dissociation constant of 5.9 microM at 38°C.

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    Area of Science:

    • Pharmacokinetics
    • Biochemistry
    • Drug-protein interactions

    Background:

    • Erythromycin is a widely used antibiotic.
    • Understanding its binding to human serum is crucial for pharmacokinetics.
    • Serum protein binding influences drug distribution and efficacy.

    Purpose of the Study:

    • To characterize the binding of erythromycin to human serum.
    • To determine the binding parameters, including affinity and thermodynamics.
    • To investigate the influence of pH and serum concentration on binding.

    Main Methods:

    • Measurement of erythromycin binding to human serum at equilibrium.
    • Assessment of binding sensitivity to pH variations.
    • Determination of the relationship between bound fraction and serum dilution.

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  • Kinetic and thermodynamic analysis of binding parameters.

    • Main Results:

    • Erythromycin binding is pH-dependent, decreasing at acidic pH.
    • Binding is completely reversible and exhibits a semilogarithmic relationship with serum concentration.
    • A specific, saturable binding component was identified, indicating a single class of noninteracting sites.
    • Apparent dissociation constant (Kd) was 5.9 microM at 38°C and 8.4 microM at 25°C.

    Conclusions:

    • Erythromycin specifically binds to human serum proteins at a defined site.
    • The binding process is reversible and influenced by physiological conditions like pH.
    • Thermodynamic parameters suggest an entropy-driven binding process.