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Bovine serum albumin is a monomeric, water-soluble plasma protein made up of a single chain of 583 amino acids, with a molecular weight of approximately 66.5 kDa. It consists of three homologous domains (I, II, III), each divided into two subdomains, forming a heart-shaped molecule primarily composed of α-helices. BSA binds a wide variety of small molecules including fatty acids, hormones, bilirubin, and drugs, and is essential for maintaining oncotic pressure and stabilizing extracellular fluid volume in bovine blood. It is highly soluble, stable, and widely used as a protein standard, stabilizer, and carrier in research and industrial applications. While allergenic, BSA is generally considered to be non-toxic and non-antigenic in laboratory use, with its structure well-resolved by crystallography. It is not a drug target, but its ligand-binding properties make it valuable for studying drug-protein interactions and pharmacokinetics.
Non-specific binding of ligands via hydrophobic and electrostatic interactions. Uptake and transport of bound small molecules and drugs.
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