Publication

Abstract : Human Serum Albumin (HSA) is a prominent protein in plasma. Protein binds with different types of ligands such as fatty acids, drugs and surfactants. Interaction of serum albumin and bile salts is studied, due to its important application in drug delivery and biopharmaceuticals. The bile salts are amphibilic molecules, synthesized by liver and undergo aggregation in aqueous media. In the present work, sodium cholate (NaC) is used as model bile salt. The interaction of NaC and HSA is monitored using intrinsic Trp-214 fluorescence. Urea (U) ([U] = 0–9.6 M) is added to the pre-formed HSA-NaC system to study. The association of NaC with Trp 214, which is buried within the hydrophobic core of sub domain IIA (Sudlow site I) of HSA, shows a prominent nature of maintaining the protein in the native conformation and hence there is very minimal change in photophysical properties of HSA-NaC system. The denaturation study carried out on HSA-NaC system by using chemical denaturant urea, shows very minimal change in the photophysical property of Trp 214, up to a 6 M concentration of U. Whereas, from 7.2 to 9.6 M [U] the fluorescence intensity show a decrease along with a 3 nm red shift.