Denaturation studies on bovine serum albumin-bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity.

Protein denaturation is under intensive research, since it leads to neurological disorders of severe consequences. Avoiding denaturation and stabilizing the proteins in their native state is of great importance, especially when proteins are used as drug molecules or vaccines. It is preferred to add pharmaceutical excipients in protein formulations to avoid denaturation and thereby stabilize them.

Bile salt induced solubilization of methylene blue: Study on methylene blue fluorescence properties and molecular mechanics calculation.

Methylene blue (MB) is a hydrophobic drug molecule, having importance both as a staining reagent and pharmaceutical agent. MB is strongly fluorescent, with an emission peak at 686 nm ( 665 nm). In the study, the possibility of MB as an extrinsic fluorophore to study the micellization behavior of bile salts (BSs) was carried out.

Photophysical behavior of a new cholesterol attached coumarin derivative and fluorescence spectroscopic studies on its interaction with bile salt systems and lipid bilayer membranes.

A new fluorescent-cholesterol (Cum-Chl) molecule has been synthesized by attaching 3-acetyl-7-(diethylamino)-2H-chromen-2-one (Cum) to cholesterol via cholesterol bound β-keto ester. The β-keto ester was synthesized from the corresponding nitrile by applying the Blaise reaction. The molecule forms H-aggregates in solutions.