Fluorescence resonance energy transfer from serum albumins to 1-anthracene sulphonate entrapped in reverse micellar nanocavities

Fluorescence resonance energy transfer (FRET) between anionic probe 1-anthracene sulphonate (1-AS) and transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA) solubilized in reverse micelles of sodium 1,4-bis (2-ethylhexyl) sulphosucccinate (AOT) in heptane was studied where the donor and acceptor pair comes in close proximity within the smaller water pools. The mechanism of fluorescence quenching of transport proteins by 1-AS in reverse micelles has been ascribed to the non-radiative energy transfer process. The probable binding site of the probe with proteins has been ascertained from FRET study. Circular dichroism study suggests that the number of folding of the protein increases markedly due to binding of the proteins with 1-AS.