Scrutinzing the interaction of bovine serum albumin and human hemoglobin with isatin-triazole functionalized rhodamine through spectroscopic and In-silico approaches

A Rhodamine-based fluorescent probe R1 has been successfully utilized to detect BSA and HHb proteins via non-covalent bonding. The protein binding nature with R1 has been unravelled by the characteristic changes in absorption, emission and circular dichroism spectra that indicated their noticeable interaction. The experimental results have also shown the moderate strength between proteins and R1 from the quenching of proteins through the static quenching mechanism. The hyperchromism in the absorption band of proteins with R1 has given vital information and binding affinity values have been calculated from Stern-Volmer plots. The calculated values of the thermodynamic parameters revealed a spontaneous binding processes occurring primarily via hydrogen bonding and van der Waal interactions. Furthermore, in silico approaches have been utilized to make a comparison and conclusion with spectroscopic results. The outcome of these studies could be useful to examine the drug-protein binding for further exploitation. (C) 2022 Elsevier B.V. All rights reserved.