PMC:7152911 / 107913-111958
Annnotations
{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7152911","sourcedb":"PMC","sourceid":"7152911","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7152911","text":"3.4 Secondary binding approaches\nElectrochemical biosensors would ideally produce sensitive and selective results using label-free protocols. However, secondary binding reactions are sometimes required to facilitate the robust detection of pathogens that lack initial labels depending on the biosensor characteristics and measurement demands. Secondary binding steps can facilitate target labeling, biosensor signal amplification, and verification of target binding. Secondary binding steps provide useful in situ controls and can increase sensitivity, LOD, dynamic range, and measurement confidence (e.g., verification of target binding). Secondary binding steps also provide opportunities for acquiring additional bioanalytical information about the target species.\nHere, we classify assays that use secondary binding steps as labeled approaches in Table 1, Table 2 regardless of if the primary binding step produced a response. There is, however, a more subtle distinction if binding of the secondary species is used for amplification or verification purposes as previously discussed. Labels often include a biorecognition element-enzyme or -nanoparticle conjugate. In electrochemical biosensing applications, such labels often serve the purpose of altering the material properties or transport processes of the electrode-electrolyte interface, often by inducing a secondary reaction. Secondary binding of optically-active nanomaterials to captured targets can also enable the use of optical transducers for simultaneous detection or bioanalysis. Enzymes are among the most commonly used secondary binding species for label-based pathogen detection. As shown in Table 2, electrochemical biosensors for pathogen detection that employ enzymes are commonly performed as a sandwich assay format. A schematic of secondary binding steps for biosensor amplification based on the binding of HRP-antibody conjugates is shown in Fig. 6 a (Kokkinos et al. 2016). Hong et al. used HRP-labeled secondary antibodies to amplify the CV and EIS responses of a concanavalin A-functionalized nanostructured Au electrode to detect norovirus (Hong et al. 2015). Gayathri et al. used an HRP-antibody conjugate to induce an enzyme-assisted reduction reaction with an immobilized thionine-antibody receptor in an H2O2 system for detection of E. coli down to 50 CFU/mL using a sandwich assay format (Gayathri et al. 2016). Xu et al. used glucose oxidase and monoclonal anti-S. typhimurium to functionalize magnetic bead labels for separation and detection of S. typhimurium on an Au IDAM using EIS and glucose to catalyze the reaction that exhibited a linear working range of 102 to 106 CFU/mL (Xu et al. 2016b).\nFig. 6 Highlight of secondary binding and signal amplification approaches utilized in electrochemical biosensor-based pathogen detection. a) Four amplification approaches associated with the secondary binding of enzyme-labeled secondary antibodies: (A) electron transfer mediation; (B) nanostructuring of surface for increased rate of charge transfer kinetics; (C) conversion of electrochemically inactive substrate into a detectable electroactive product; (D) catalysis of oxidation of glucose for production of hydrogen peroxide for electrochemical detection (Kokkinos et al. 2016). b) Signal amplification via non-selective binding of AuNPs to bound bacterial target (E. coli) (Wan et al. 2016).\nIn addition to enzymes, secondary binding of nanoparticles has also been used for pathogen detection. As shown in Fig. 6b, Wan et al. utilized non-functionalized AuNPs to amplify the EIS response of an antibody-immobilized planar Au electrode to E. coli detection (Wan et al. 2016). A detailed overview of studies that employ enzymes and nanoparticles is provided in Table 2. We remind the reader that while secondary binding steps are useful techniques, assays that avoid secondary binding steps have advantages for bioprocess monitoring and control applications, as they avoid the addition of reagents to a process that may compromise product 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