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Serum albumin is the most abundant protein in human plasma, accounting for approximately 50-60% of total protein content. It plays a critical role in maintaining the colloid osmotic pressure required for proper fluid distribution between the intravascular and extravascular compartments [1, 2]. Beyond its hemodynamic functions, albumin and other carrier proteins like transthyretin and sex hormone-binding globulin serve as essential transporters for a wide array of ligands, including fatty acids, hormones, metal ions, and pharmaceutical agents [3, 4]. In clinical practice, albumin is used as a therapeutic agent for volume expansion in conditions like cirrhosis or severe burns [8]. Furthermore, its high binding capacity is exploited in drug development through 'nab-technology' (nanoparticle albumin-bound) to enhance the delivery and efficacy of hydrophobic drugs like paclitaxel [7]. Understanding the binding affinity of drugs to these proteins is vital, as only the unbound fraction is pharmacologically active, and competition for binding sites can lead to significant drug-drug interactions [5, 6].
Acts as a primary transport vehicle for endogenous and exogenous compounds, regulates blood volume through oncotic pressure, and serves as a drug delivery scaffold to improve solubility and half-life.
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