“ AXT binding to the protein produced significant alterations in both secondary and tertiary structures of HSA , as revealed from the far-UV and the near-UV CD spectral results.”
“Fluorescence quenching titration results demonstrated moderately strong binding affinity between AXT and HSA based on the binding constant value (1.08±0.06×10(5)M(-1)), obtained in 10mM sodium phosphate buffer, pH7.4 at 25°C.”
“This was also confirmed from alteration in the UV-vis spectrum of HSA upon AXT addition.”
“Three-dimensional fluorescence spectral results indicated significant microenvironmental changes around Trp and Tyr residues of HSA upon complexation with AXT.”