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Related Experiment Videos

Nimesulide binding to components within blood

F Bree1, P Nguyen, S Urien

  • 1Département de Pharmacologie, Faculté de Médecine de Créteil, Université de Paris XII, France.

Drugs
|January 1, 1993
PubMed
Summary
This summary is machine-generated.

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Nimesulide extensively binds to human serum proteins, primarily albumin, with minimal erythrocyte binding. Its free fraction remains constant therapeutically, though certain drugs and its metabolite can alter binding.

Area of Science:

  • Pharmacology
  • Biochemistry

Background:

  • Nimesulide is a non-steroidal anti-inflammatory drug (NSAID).
  • Understanding drug binding to serum proteins is crucial for predicting efficacy and toxicity.

Purpose of the Study:

  • To investigate the binding of nimesulide to human serum proteins and erythrocytes.
  • To identify factors affecting nimesulide binding, including other drugs and metabolites.

Main Methods:

  • Equilibrium dialysis was employed to study nimesulide binding.
  • Interactions with specific binding site markers on serum albumin were assessed.

Main Results:

  • Nimesulide exhibits high (99%) non-saturated binding to serum, predominantly to albumin.
  • Erythrocyte binding is moderate in buffer but negligible in whole blood.

Related Experiment Videos

  • Valproic acid, fenofibrate, and the metabolite 4-hydroxy-nimesulide can displace nimesulide.
  • Nimesulide binds to two distinct sites on albumin, with higher affinity for site II.

    • Conclusions:

    • Nimesulide's high serum protein binding influences its distribution.
    • Altered binding in renal failure and hepatic cirrhosis warrants consideration.
    • Potential for drug displacement by valproic acid and fenofibrate necessitates caution.