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The plasma protein binding of basic drugs.

P A Routledge

    British Journal of Clinical Pharmacology
    |November 1, 1986
    PubMed
    Summary

    Plasma protein binding of basic drugs varies due to differences in alpha-1-acid glycoprotein (AAG). Changes in AAG affect drug distribution and metabolism, complicating treatment efficacy and toxicity assessments.

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    Area of Science:

    • Pharmacokinetics
    • Drug Metabolism
    • Clinical Pharmacology

    Background:

    • Plasma protein binding significantly influences drug disposition and efficacy.
    • Alpha-1-acid glycoprotein (AAG) is a key protein binding basic drugs.
    • Variability in AAG levels impacts drug response.

    Purpose of the Study:

    • To investigate the variability in plasma protein binding of basic drugs.
    • To understand the role of alpha-1-acid glycoprotein (AAG) in this variability.
    • To explore the clinical implications of AAG concentration changes on drug efficacy and toxicity.

    Main Methods:

    • Analysis of plasma protein binding assays for basic drugs.
    • Measurement of AAG concentrations in patient populations.
    • Correlation analysis between AAG levels and drug concentrations.

    Main Results:

    • Significant intra- and interindividual variability in basic drug plasma protein binding was observed.
    • AAG concentration directly correlates with the extent of basic drug binding.
    • Altered AAG levels lead to changes in drug distribution and metabolism.

    Conclusions:

    • Plasma protein binding of basic drugs is highly variable, primarily due to AAG fluctuations.
    • Monitoring AAG levels is crucial for interpreting total drug concentrations and predicting clinical outcomes.
    • Direct measurement of free drug concentrations, though challenging, may enhance therapeutic drug monitoring for certain agents like lignocaine.

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