Resolving interactions of miglitol with normal and glycated human serum albumin by multivariate methods

This article reports results of one of our projects related to the investigation of interactions of miglitol (MIG) with normal human serum albumin (HSA) and glycated HSA (GHSA) with the help of recording spectroscopic and electrochemical data. The experimental data were analyzed by conventional and chemometric methods to extract useful information for comprehensive justifications of the interactions of the MIG with HSA and GHSA. Hard-and soft-modeling chemometric methods were used to extract quantitative and qualitative information. Then, mo-lecular docking techniques were used to further investigation of the binding of the MIG with HSA and GHSA and the extracted results were compatible with those obtained by experimental methods. Finally, according to the binding of the BV with HSA and GHSA, second-order differential pulse voltammetric data were recorded and calibrated with three-way calibration methods for exploiting second-order advantage for determination of the GHSA in the presence of the HSA to develop a novel chemometrics assisted-electroanalytical method for diag-nostic and monitoring of diabetic.

Automated summary

This article discusses the investigation of interactions between miglitol and normal human serum albumin and glycated HSA, using spectroscopic and electrochemical data. Chemometric methods were employed to extract useful information for justifying these interactions, and molecular docking techniques were used for further investigation. A novel chemometrics-assisted electroanalytical method was developed for diagnostic and monitoring of diabetes.