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Despite the indisputable benefits and advancement of science, technology, and civilization, early diagnosis of healthcare is still a challenging field for the scientific fraternity. The detection of biomarkers is a crucial attribute of prognosis and diagnosis of disease. Out of numerous techniques, surface plasmon resonance (SPR) bestows countless benefits, including in situ, label-free, and real-time assessment, etc., which authorizes the analysis of molecular binding occurrences between biotransducers and biomarkers. In addition, SPR with low-molecular-weight biomarkers lacks selectivity and sensitivity, which ultimately affects binding kinetics. This, in turn, leads to the remarkable development and implementation of numerous selectivity and sensitivity enhancement methods. Among the various noticeable strategies, because of selectivity and sensitivity enrichment substrate for SPR biosensors, affinity-based nanoarchitectured biotransducers stand out as being the best substitute. The present review elaborates significant advances made in the research based on affinity biotransducers for in vitro diagnosis using SPR biosensors for biomarker sensing. Moreover, most recent trends and challenges in designing and application of nanoarchitectured affinity biotransducer-based SPR biosensors for detecting low-concentration biomarkers have been reviewed comprehensively. This present review may assist the scientific fraternity in designing an ultramodern novel SPR approach based on affinity biotransducers, along with improved selectivity and sensitivity of SPR biosensors for in vitro and real-time diagnostic applications.
Despite the indisputable benefits and advancement of science, technology, and civilization, early diagnosis of healthcare is still a challenging field for the scientific fraternity. The detection of biomarkers is a crucial attribute of prognosis and diagnosis of disease. Out of numerous techniques, surface plasmon resonance (SPR) bestows countless benefits, including in situ, label-free, and real-time assessment, etc., which authorizes the analysis of molecular binding occurrences between biotransducers and biomarkers. In addition, SPR with low-molecular-weight biomarkers lacks selectivity and sensitivity, which ultimately affects binding kinetics. This, in turn, leads to the remarkable development and implementation of numerous selectivity and sensitivity enhancement methods. Among the various noticeable strategies, because of selectivity and sensitivity enrichment substrate for SPR biosensors, affinity-based nanoarchitectured biotransducers stand out as being the best substitute. The present review elaborates significant advances made in the research based on affinity biotransducers for in vitro diagnosis using SPR biosensors for biomarker sensing. Moreover, most recent trends and challenges in designing and application of nanoarchitectured affinity biotransducer-based SPR biosensors for detecting low-concentration biomarkers have been reviewed comprehensively. This present review may assist the scientific fraternity in designing an ultramodern novel SPR approach based on affinity biotransducers, along with improved selectivity and sensitivity of SPR biosensors for in vitro and real-time diagnostic applications.
The introduction of spacers in coating steroid protein complex and / or enzyme conjugates or immunogen is known to exert an influence on the sensitivity of steroid enzyme immunoassays. We have introduced different homobifunctional spacers between enzyme and prednisolone (PSL) moiety having atomic length 3 to 10 and studied their influence on functional parameters such as sensitivity and specificity of PSL enzyme immunoassays. In this study, four enzyme conjugates of PSL-21-HS and HRP were prepared by N-Hydroxy Succinimide mediated carbodiimide reaction, these were PSL-21-HS-adipic acid dihydrazide (ADH)-HRP, PSL-21-HS- carbohydrazide (CH)-HRP, PSL-21-HS-ehylenediamine (EDA)-HRP and PSL-21-HS- urea (U)-HRP. The assays were developed using these enzymes conjugate with antibody raised against PSL-21-HS-BSA immunogen. The sensitivity of the PSL assays after insertion of bridge in enzyme conjugate were 1.22 ng/mL, 0.59 ng/mL, 0.48 ng/mL and 0.018 ng/mL with ADH, CH, EDA and urea as spacer respectively. Among all four combinations, PSL-21-HS-BSA antibody and PSL-21-HS-U-HRP enzyme conjugate gave better sensitivity and showed cross-reaction with less number of steroids. The percent recovery of PSL from the exogenously spiked human serum pools was in the range of 88.32-102.50 %. The intra and inter assay CV % was < 8.46%. The PSL concentration was estimated in the serum samples of patients on PSL treatment. The serum PSL values obtained by this method correlated well with the commercially available kit (r2 = 0.98). The present study, suggests that the nature of the spacer is related to assay sensitivity and not the spacer length.
The introduction of spacers in coating steroid protein complexes and/or enzyme conjugates or immunogens is known to exert an influence on the sensitivity of steroid enzyme immunoassays. We investigated the impact of different homobifunctional spacers, ranging in atomic length from 3 to 10, on the sensitivity and specificity of prednisolone (PSL) enzyme immunoassays. In this study, four homo-bifunctional spacers, namely, carbohydrazide (CH), adipic acid dihydrazide (ADH), ethylene diamine (EDA), and urea (U), were incorporated between PSL and horseradish peroxidase (HRP) for preparing the enzyme conjugate with an aim to improve the sensitivity of the assay without compromising assay specificity. The assays were developed using these enzymes conjugated with antibodies raised against the PSL-21-HS-BSA immunogen. The sensitivity of the PSL assays after insertion of a bridge in the enzyme conjugate was 1.22 ng/mL, 0.59 ng/mL, 0.48 ng/mL, and 0.018 ng/mL with ADH, CH, EDA, and urea as a spacer, respectively. Among the four combinations, the PSL-21-HS-BSA-antibody with PSL-21-HS-U-HRP-enzyme conjugate gave better sensitivity and less cross-reaction. The percent recovery of PSL from the exogenously spiked human serum pools was in the range of 88.32%-102.50%. The intra and inter-assay CV% was< 8.46%. The PSL concentration was estimated in the serum samples of patients on PSL treatment. The serum PSL values obtained by this method correlated well with the commercially available kit (r2 = 0.98). The present study suggests that the nature of the spacer is related to assay sensitivity and not the spacer length.
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