Interaction of Bovine Serum Albumin with Dipolar Molecules: Fluorescence and Molecular Docking Studies

• DOI: 10.1021/jp808611b
• Publication Date: 2009-01-28T13:35:07Z
• Authors: Bhaswati Bhattach...; Srinivas Nakka; Lalitha Guruprasad; Anunay Samanta
• Keywords: Bovine serum albumin; Docking (animal)

Interaction of bovine serum albumin (BSA) with two series dipolar molecules having both rigid and flexible structures has been studied by monitoring the spectral temporal behavior intramolecular charge transfer fluorescence systems. The binding sites molecular systems in BSA have located help docking studies. Three different varying hydrophobicity identified where these are located. Binding hydrophobic domains leads to a blue shift spectra an enhancement intensity lifetime. This is found be largest for which internal motion serves as nonradiative decay route. In BSA-bound condition, some exhibit not-so-common "dip-rise-dip" time-resolved anisotropy profiles. It shown that large difference lifetimes protein-bound unbound one factors contributes this kind As often responsible short lifetime molecules, increase occurs if disruption/prevention motion. thus appears it might possible obtain information on prevention/disruption pathway protein from profiles discussed above. However, since present study reveals cases change also due other reasons, needs careful prior making any conclusion.