Developing a novel amperometric method for biosensing of carbonic anhydrase II based on conventional and multi-way chemometric analyses of its inhibition by acetazolamide, dorzolamide and methazolamide

In this work, we were going to generate first- and second-order electrochemical and spectroscopic data to investigate inhibition of the carbonic anhydrase II (CA II) by acetazolamide (AZ), dorzolamide (DZ) and methazolamide (MZ) which enabled us to have a deep insight to the mechanism of these inhibitions. MCR-ALS and PARAFAC were chosen for chemometric analyses of the data and after data resolution, spectral and voltammetric profiles and concentration profiles were obtained which helped us to obtain qualitative information about inhibition of the CA II which was completed by molecular docking and hard-modeling of the data. Our results showed that order of the inhibition of the CA II was occurred according to MZ > DZ > AZ. According to the results of inhibition of the CA II, the MZ was used to develop a novel amperometric method for determination of the CA II which was not electroactive. The sensor response was linearly correlated with concentration of the CA II in the range of 0–20 nM with a limit of detection (LOD) of 0.21 nM and a sensitivity of 0.57 μA nM−1. The developed method was stable, selective and sensitive for the determination of the CA II. •Binding and inhibition of the carbonic anhydrase II by three drugs were investigated.•Electrochemical and spectroscopic data were collected and analyzed.•Experimental evidence were completed by theoretical evidence.•Our results confirmed inhibition of the carbonic anhydrase II was occurred in an order of MZ > DZ > AZ.•Finally, an electrochemical method was developed for determination of the CA II.