期刊
JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS
卷 156, 期 -, 页码 23-35出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jpba.2018.04.021
关键词
Tasmar; Human serum albumin; Interaction; Matrix augmentation; Hard modeling; Amperometric biosensing
资金
- Research Council of Kermanshah University of Medical Sciences
In this work, voltammetric data recorded by a glassy carbon electrode (GCE) was used to investigate the interactions of tolcapone (Tasmar, TAS) with human serum albumin (HSA) at the electrode surface. The recorded voltammetric data was also combined with spectroscopic data to construct an augmented data matrix which was analysed by multivariate curve resolution-alternating least squares (MCR-ALS) as an efficient chemometric tool to obtain more information about TAS-HSA interactions. The results of MCR-ALS confirmed formation of one complex species (HSA-TAS2) and application of MCR-BANDS to the results of MCR-ALS confirmed the absence of rotational ambiguities and existing unambiguous and reliable results. Binding of TAS to HSA was also modeled by molecular docking and the results showed that the TAS was bound to sub-domain IIA of HSA which were compatible with the ones obtained by recording experimental data. Hard-modeling of combined voltammetric and spectroscopic data by EQUISPEC helped us to compute binding constant of HSA-TAS2 complex species which was compatible with the binding constant value obtained by direct analysis of experimental data. Finally, a new electroanalytical method was developed based on TAS-HSA interactions for determination of HSA in two ranges of 0-541 nM and 541-1200 nM with a limit of detection of 0.04 nM and a sensitivity of 0.02 mu A nM(-1). (C) 2018 Elsevier B.V. All rights reserved.
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