Fluorescence resonance energy transfer A promising tool for investigation of the interaction between 1-anthracene sulphonate and serum albumins

This present investigation has revealed that steady state as well as time-resolved fluorescence techniques can serve as highly sensitive monitors for exploring the interaction of fluorescent probe 1-anthracene sulphonate (1-AS) with model transport proteins bovine serum albumin (BSA) and human serum albumin (HSA) We have focused on fluorescence resonance energy transfer (FRET) between excited tryptophan in transport proteins to 1-AS for the study of relaxation dynamics of biological molecules (C) 2010 Elsevier BV All rights reserved