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      Electrochemical Immunosensor Based on Polythionine/Gold Nanoparticles for the Determination of Aflatoxin B 1

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          Abstract

          An aflatoxin B 1 (AFB 1) electrochemical immunosensor was developed by the immobilisation of aflatoxin B 1-bovine serum albumin (AFB 1-BSA) conjugate on a polythionine (PTH)/gold nanoparticles (AuNP)-modified glassy carbon electrode (GCE). The surface of the AFB 1-BSA conjugate was covered with horseradish peroxidase (HRP), in order to prevent non-specific binding of the immunosensors with ions in the test solution. The AFB 1 immunosensor exhibited a quasi-reversible electrochemistry as indicated by a cyclic voltammetric (CV) peak separation (ΔE p) value of 62 mV. The experimental procedure for the detection of AFB 1 involved the setting up of a competition between free AFB 1 and the immobilised AFB 1-BSA conjugate for the binding sites of free anti-aflatoxin B 1 (anti-AFB 1) antibody. The immunosensor's differential pulse voltammetry (DPV) responses (peak currents) decreased as the concentration of free AFB 1 increased within a dynamic linear range (DLR) of 0.6 - 2.4 ng/mL AFB 1 and a limit of detection (LOD) of 0.07 ng/mL AFB 1. This immunosensing procedure eliminates the need for enzyme-labeled secondary antibodies normally used in conventional ELISA–based immunosensors.

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          IARC monographs on the evaluation of carcinogenic risks to humans. Ingested nitrate and nitrite, and cyanobacterial peptide toxins.

          (2010)
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            Electrochemical immunosensor array using a 96-well screen-printed microplate for aflatoxin B1 detection.

            D Moscone, N Ammida, Teresa L. Micheli … (2007)
            A novel analytical immunosensor array, based on a microtiter plate coupled to a multichannel electrochemical detection (MED) system using the intermittent pulse amperometry (IPA) technique, is proposed for the detection of aflatoxin B1 (AFB1). In the present work, the electrochemical behaviour and electroanalytical performance of the thick-film carbon sensors (also designated as screen-printed electrodes) incorporated in the multichannel electrochemical plate were first evaluated. Then the 96-well screen-printed microplate was modified in accord with a competitive indirect enzyme-linked immunoassay (ELISA) format for aflatoxin B1 detection. The measurements were performed using both spectrophotometric and electrochemical procedures and the results of the calibration curves, detection limit (LOD), sensitivity and reproducibility of the respective assay systems were evaluated. The immunoassay was then applied for analysis of corn samples spiked with AFB1 before and after the extraction treatment, in order to study the extraction efficiency and the matrix effect, respectively. These studies have shown that using this system, AFB1 can be measured at a level of 30 pg/mL and with a working range between 0.05 and 2 ng/mL. Good recoveries (103+/-8%) were obtained, demonstrating the suitability of the proposed assay for accurate determination of the AFB1 concentration in corn samples. The specificity of the assay was assessed by studying the cross-reactivity of PAb relative to AFB1. The results indicated that the PAb could readily distinguish AFB1 from other aflatoxins, with the exception for AFG1.
            Article 0 comments Cited 35 times – based on 0 reviews     Review now
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              Direct competitive ELISA based on a monoclonal antibody for detection of aflatoxin B1. Stabilization of ELISA kit components and application to grain samples.

              Kyung Won Shim, O Kolosova, Seon Hwa Chung … (2005)
              A direct competitive enzyme-linked immunosorbent assay (ELISA) based on a monoclonal antibody has been developed and optimized for detection of aflatoxin B1 (AFB1), and an ELISA kit has been designed. This immunoassay was highly specific, sensitive, rapid, simple, and suitable for aflatoxin monitoring. AFB1 concentrations determinable by ELISA ranged from 0.1 to 10 microg L(-1). The IC50 value was 0.62 microg L(-1). Recovery from spiked rice samples averaged between 94 and 113%. The effect of different reagents on the stability of HRP-AFB1 conjugate solution was studied. The performance of a stabilized enzyme tracer in ELISA was determined and compared with that of a freshly prepared control solution of HRP-AFB(1) conjugate. The results showed that stabilizing media containing 0.02% BSA, 0.1% Kathon CG, and 0.05 mol L(-1) calcium chloride in 0.05 mol L(-1) Tris-HCl buffer (pH 7.2) maintained the activity of HRP-AFB1 at a dilution of 1:1000 for a period of at least 12 months at room temperature whereas the reference conjugate solution without the additives lost its activity within a few days. Several additives were tested for their stabilizing effect on a monoclonal antibody (MAb) immobilized on the surface of polystyrene microtitre plates. It was shown that immobilized MAb, treated with post-coating solutions containing PVA, BSA, and combinations of these substances with trehalose, retained its activity for at least 4 months at 4 degrees C, whereas the untreated MAb-coated plate lost its activity within 2 days.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Sensors (Basel)
                Journal ID (iso-abbrev): Sensors (Basel)
                Title: Sensors (Basel, Switzerland)
                Publisher: Molecular Diversity Preservation International (MDPI)
                ISSN (Electronic): 1424-8220
                Publication date Collection: December 2008
                Publication date (Electronic): 15 December 2008
                Volume: 8
                Issue: 12
                Pages: 8262-8274
                Affiliations
                SensorLab, Department of Chemistry, University of Western Cape, Private Bag X17, Bellville 7535, Cape Town, South Africa
                Author notes
                [* ] Author to whom correspondence should be addressed; E-mail: eiwuoha@ 123456uwc.ac.za
                Article
                Publisher ID: sensors-08-08262
                DOI: 10.3390/s8128262
                PMC ID: 3791018
                PubMed ID: 27873987
                SO-VID: d9a33b88-2a30-4e03-a5fc-fd4308b0f1e3
                Copyright © © 2008 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.
                License:

                This article is an open-access article distributed under the terms and conditions of the CreativeCommons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 19 September 2008
                Date revision received : 01 December 2008
                Date accepted : 02 December 2008
                Categories
                Subject: Article

                ScienceOpen disciplines: Biomedical engineering
                Keywords: aflatoxin b1,horseradish peroxidise (hrp),gold nanoparticles,polythionine,immunosensor
                Data availability:
                ScienceOpen disciplines: Biomedical engineering
                Keywords: aflatoxin b1, horseradish peroxidise (hrp), gold nanoparticles, polythionine, immunosensor

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