ABSTRACT
Albumin is the most profuse blood protein. It serves as a reservoir and is also involved in the transport of a plethora of substances like nutrients, hormones, metals, and toxins. Albumin is produced mostly in liver hepatocytes. It has a molecular weight of 66.5 kDa, and its half-life is 19 days. It is. Albumin is available in three variants, i.e., ovalbumin, bovine serum albumin (BSA), and human serum albumin (HSA). Monomeric phosphoglycoprotein, ovalbumin finds immense application in food and drug delivery because of its easy availability, low cost, emulsion stabilization as well as pH/temperature responsive behavior. BSA is also extensively used in drug delivery because of its extraordinary ligand binding capacity. The most abundant hydrophilic plasma protein, HSA is another important component in different drug delivery system because of its inert and biodegradable nature with significant internalization in tumor and inflamed tissues.
These features of albumin make it an ideal candidate for half-life enhancement and site-directed delivery of bioactives associated by covalent conjugation, genetic fusions, or ligand-mediated interactions. The ability to the covalent or non-covalent attachment of the drug to albumin or encapsulation of drug into albumin nanoparticle depending on physical 34interaction gives a range of design option that has entered clinical trials or already in the market. This chapter will provide a spotlight on albumin structure and binding sites, a molecular association of albumin and the role of albumin in drug transport for the formulation design of next-generation drug delivery systems.
