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Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
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Protein-drug binding, a pivotal aspect of pharmacokinetics, is subject to considerable variability influenced by an array of patient-related factors. The intricate interplay of age, individual differences, and pathological conditions significantly impact the binding dynamics and subsequent pharmacological effects.
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Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
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Accounting for Differences in Plasma Protein Binding between Fish and Humans for Supporting Environmental Risk

A Ross Brown1, Maciej Trznadel1, Siffreya Pedersen1

  • 1Biosciences, Faculty of Health and Life Sciences, University of Exeter, Stocker Road, Exeter, Devon EX4 4QD, United Kingdom.

Environmental Science & Technology
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Active pharmaceutical ingredients (APIs) have higher unbound fractions in fish plasma than humans, especially anionic APIs in rainbow trout. Accounting for these differences improves environmental risk assessments using the Fish Plasma Model (FPM).

Keywords:
AGPalbuminapolipoproteinsblood plasmacyprinid fishionizable pharmaceuticalssalmonid fish

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Area of Science:

  • Environmental chemistry
  • Ecotoxicology
  • Pharmacokinetics

Background:

  • The Fish Plasma Model (FPM) estimates environmental risk by comparing fish plasma concentrations of active pharmaceutical ingredients (APIs) to human therapeutic levels.
  • This model assumes conserved pharmaceutical targets and does not account for species-specific differences in plasma protein binding, which affects API bioavailability.

Purpose of the Study:

  • To quantify the unbound fraction (fu) of 44 APIs in three fish species (rainbow trout, fathead minnow, koi carp) and compare it to human fu.
  • To investigate the influence of fish blood physicochemistry and composition on interspecies differences in API binding.
  • To provide recommendations for refining the FPM for more accurate environmental risk assessment.

Main Methods:

  • Quantification of fu for 44 APIs across a range of physicochemical properties in rainbow trout, fathead minnow, and koi carp.
  • Comparison of fish fu values with human fu data.
  • Analysis of interspecies fu variations in relation to fish blood composition (proteins, lipids, etc.).

Main Results:

  • Anionic APIs exhibited significantly higher fu (up to 10-fold) in fish compared to humans.
  • Rainbow trout showed the most pronounced differences in fu for anionic APIs, despite having proteins similar to human serum albumin.
  • Significant correlations were observed between fu and fish blood characteristics, indicating species-specific binding.

Conclusions:

  • The unbound fraction (fu) of APIs in fish plasma differs substantially from humans, particularly for anionic compounds.
  • Incorporating species-specific fu values, especially from conservative species like rainbow trout, is crucial for accurate environmental risk assessment using the FPM.
  • Current FPM approaches may overestimate API exposure and risk in aquatic organisms due to neglecting interspecies differences in plasma protein binding.