Characterization of the interaction of diosgenin with human serum albumin and α1-acid glycoprotein using biophysical and bioinformatic tools

摘要: Abstract Diosgenin (DIO), a steroidal sapogenin with high therapeutic potential, has been shown to exhibit myriad of pharmacologically significant properties and is commonly used as template for synthesizing drugs. The efficacy bioactive compounds potential drug depends mainly upon their interaction proteins in the circulatory system. Therefore, DIO major carrier humans, i.e. human serum albumin (HSA) α1-acid glycoprotein (AAG), was characterized using multispectroscopic molecular docking techniques. Analysis fluorescence enhancement data showed intermediate binding affinity both DIO–HSA DIO–AAG interactions. Circular dichroism spectral results revealed minimal conformational alterations HSA binding, but effect on AAG more significant. Competitive ligand displacement suggested that does not bind strongly main sites HSA. However, found favor subdomain IB based data. For AAG, location determined two variants (A F1*S variants) docking. variant A, site situated lobes I II central pocket protein, while F1*S, docked cleft protein surface. Hydrophobic interactions van der Waals forces were responsible complexation between proteins. Additionally, there involvement hydrogen bonding