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Protein binding of diclofenac

01

Overview

"Protein binding of diclofenac" refers to the high-affinity reversible association between diclofenac—a nonsteroidal anti-inflammatory drug—and plasma proteins, primarily serum albumin, with more than 99% bound under normal physiological conditions[1][4]. This process is not itself a therapeutic target but rather an important pharmacokinetic property that influences the distribution, elimination, and free active concentration of diclofenac in circulation. The extent and nature of this protein-drug interaction are clinically significant because only unbound ("free") diclofenac is pharmacologically active. Factors such as disease state (e.g., liver/kidney impairment), competition from other highly bound drugs, changes in pH, or alterations in serum albumin levels can affect this equilibrium—potentially leading to increased side effects or reduced efficacy if the proportion of unbound drug rises unexpectedly[2][3]. This entry does not represent a specific molecular entity like an enzyme or receptor; instead it describes a physicochemical property relevant to all highly protein-bound drugs.

Other names
Diclofenac plasma protein bindingDiclofenac-albumin interactionDiclofenac serum protein binding
02

Biological functions

Drug transport in blood (via albumin and other plasma proteins)Modulation of free drug concentration and pharmacokinetics
03

Disease associations

Other (affects pharmacokinetics in various disease states such as liver or kidney dysfunction)
04

Safety considerations

Altered protein binding can increase the risk of toxicity or reduce efficacy if displaced by other drugs or in disease states affecting albumin levelsChanges in free drug concentration due to altered protein binding may require dose adjustments in certain populations
05

Interacting drugs

Diclofenac

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