Effect of Protein Binding on the Dissolution of Paracetamol Using Various Proteins

Abstract

This study explores the impact of protein binding on the in vitro dissolution profile of paracetamol using dietary proteins, egg albumin and casein as model binders. Paracetamol tablets (Calpol 500 mg) were subjected to dissolution testing in phosphate buffer (pH 5.5) containing varying concentrations (50 mg, 100 mg, 150 mg) of either protein. Drug release was evaluated at multiple time intervals using UV-Visible spectrophotometry. The results demonstrated a concentration-dependent effect: at lower protein levels (50 mg), both egg albumin and casein enhanced the dissolution of paracetamol. In comparison, higher concentrations (100 mg and 150 mg) led to reduced drug release. This suggests that low protein levels may aid tablet disintegration and solubilization, while elevated protein concentrations may sequester the drug via non-covalent interactions, reducing its free, diffusible form. These findings underscore the importance of protein-drug interactions in influencing drug bioavailability and highlight the need to consider dietary or formulation-based protein content in oral drug administration.