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"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.
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