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Related Experiment Videos

Steroid-protein interactions. Human corticosteroid binding globulin: some physicochemical properties and binding

K E Mickelson, J Forsthoefel, U Westphal

    Biochemistry
    |October 13, 1981
    PubMed
    Summary

    Reducing agents affect human corticosteroid-binding globulin (CBG) binding affinity for cortisol. Steroid structure significantly influences binding, revealing key features for optimal interaction with CBG.

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    Corticosteroid-binding globulin. A review of some recent aspects.

    Molecular and cellular biochemistry·1983

    Area of Science:

    • Biochemistry
    • Molecular Endocrinology

    Background:

    • Human corticosteroid-binding globulin (CBG) plays a crucial role in regulating the bioavailability of steroid hormones.
    • Understanding the factors influencing CBG-steroid interactions is essential for endocrinology and drug development.

    Purpose of the Study:

    • To investigate the impact of reducing agents on CBG-steroid binding affinity.
    • To determine the influence of pH and temperature on the binding constants of CBG complexes.
    • To elucidate the structural requirements for optimal steroid binding to human CBG.

    Main Methods:

    • Equilibrium association constant (Ka) measurements using varying concentrations of reducing agents (dithiothreitol, beta-mercaptoethanol).
    • pH-dependent binding studies and van't Hoff analysis of temperature effects on Ka.

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  • Systematic evaluation of binding affinities for 47 different steroids.

    • Main Results:

    • Reducing agents reversibly decrease CBG-cortisol binding affinity, yielding more consistent Ka values.
    • CBG exhibits a broad pH optimum (pH 8-11) for cortisol and progesterone binding, with relative affinities varying with pH.
    • Steroid structure, particularly the 20-oxo group, 10 beta-methyl group, and 4-position double bond, significantly impacts binding energy.

    Conclusions:

    • Reducing agents can modulate CBG-steroid interactions and improve binding assay consistency.
    • The binding site of human CBG accommodates specific steroid structural features, providing insights into ligand recognition.
    • Enthalpy drives the association of cortisol and progesterone with CBG, with entropy changes compensating.