The interaction of plant-growth regulators with serum albumin: Molecular modeling and spectroscopic methods

The affinity between two plant-growth regulators (PGRs) and human serum albumin (HSA) was investigated by molecular modeling techniques and spectroscopic methods. The results of molecular modeling simulations revealed that paclobutrazol (PAC) could bind on both site I and site II in HSA where the interaction was easier, while uniconazole (UNI) could not bind with HSA. Furthermore, the results of fluorescence spectroscopy, three-dimensional (3D) fluorescence spectroscopy and circular dichroism (CD) spectroscopy suggested that PAC had a strong ability to quench the intrinsic fluorescence of HSA. The binding affinity (K-b) and the amounts of binding sites (n) between PAC and HSA at 291 K were estimated as 2.37 x 10(5) mol L-1 and 1, respectively, which confirm that PAC mainly binds on site II of HSA. An apparent distance between the Trp214 and PAC was 4.41 nm. Additionally, the binding of PAC induced the conformational changes of disulfide bridges of HSA with the decrease of a-helix content. These studies provide more information on the potential toxicological effects and environmental risk assessment of PGRs. (C) 2014 Elsevier Ltd. All rights reserved.