Exploration of twisted intramolecular charge transfer fluorescence properties of trans-2-[4-(dimethylamino)styryl]benzothiazole to characterize the protein-surfactant aggregates

► Micropolarity and microviscosity of environment around the probe in BSA-SDS aggregates is reported. ► Denaturation of protein is demonstrated by the TCSPC of DMASBT and FRET study. ► Location of the probe in the native protein and BSA-SDS aggregates is identified using FRET study. ► During unfolding of BSA, the donor-acceptor distance increases on increasing the SDS concentration. ► Anisotropy study reveals the change in conformations of BSA in the non-cooperative binding region.