Surface Plasmon Resonance Investigations of Bioselective Element Based on the Recombinant Protein A for Immunoglobulin Detection

Bakhmachuk, A. O.; Gorbatiuk, O. B.; Rachkov, A. E.; Dons’koi, Boris V.; Khristosenko, R.V.; Ushenin, Iu. V.; Peshkova, V.M.; Солдаткин, А. П.

doi:10.1186/s11671-017-1903-5

Cited by 11 publications

(5 citation statements)

References 27 publications

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“…Known bABPs are multidomain proteins, which allow high‐affinity interaction through multivalent binding. For example, SpA contains five homologous domains, each of which is capable of antibody binding and has been used in enzyme‐linked immunosorbent assay (ELISA) and surface plasmon resonance (SPR) . However, it is difficult to produce full‐length SpA in large quantities and forms poorly defined two‐to‐one antibody‐to‐SpA complexes when mixed with antibodies .…”

Section: Introductionmentioning

confidence: 99%

High‐Affinity Antibody Detection with a Bivalent Circularized Peptide Containing Antibody‐Binding Domains

Zhou

Kroetsch

Nguyen

et al. 2019

Biotechnology Journal

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Direct chemical labeling of antibody produces molecules with poorly defined modifications. Use of a small antibody-binding protein as an adapter can simplify antibody functionalization by forming a specific antibody-bound complex and introducing site-specific modifications. To stabilize a noncovalent antibody complex that may be used without chemical crosslinking, a bivalent antibody-binding protein is engineered with an improved affinity of interaction by joining two Z domains with a conformationally flexible linker. The linker is essential for the increase in affinity because it allows simultaneous binding of both domains. The molecule is further circularized using a split intein, creating a novel adapter protein ("lasso"), which binds human immunoglobulin G1 (IgG1) with K D = 0.53 nM and a dissociation rate that is 55to 84-fold slower than Z. The lasso contains a unique cysteine for conjugation with a reporter and may be engineered to introduce other functional groups, including a biotin tag and protease recognition sequences. When used in enzyme-linked immunosorbent assay (ELISA), the lasso generates a stronger reporter signal compared to a secondary antibody and lowers the limit of detection by 12-fold. The small size of the lasso and a long half-life of dissociation make the peptide a useful tool in antibody detection and immobilization.

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Section: Introductionmentioning

confidence: 99%

High‐Affinity Antibody Detection with a Bivalent Circularized Peptide Containing Antibody‐Binding Domains

Zhou

Kroetsch

Nguyen

et al. 2019

Biotechnology Journal

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“…Genetic engineering enabled the introduction of the attachment site into an expendable part of the protein, which increased the immobilization level of the molecule. The interaction between the thiol group and the surface of the gold sensor chip is much stronger and more reliable than physical adsorption [ 118 ]. Juan-Franco et al also investigated the ability of modified protein A to form an appropriate layer for enhanced immunosensing.…”

Section: Affinity-based Oriented Ab Immobilization Strategiesmentioning

confidence: 99%

Recent Advancements in Receptor Layer Engineering for Applications in SPR-Based Immunodiagnostics

Drozd

Karoń

Malinowska

2021

Sensors

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The rapid progress in the development of surface plasmon resonance-based immunosensing platforms offers wide application possibilities in medical diagnostics as a label-free alternative to enzyme immunoassays. The early diagnosis of diseases or metabolic changes through the detection of biomarkers in body fluids requires methods characterized by a very good sensitivity and selectivity. In the case of the SPR technique, as well as other surface-sensitive detection strategies, the quality of the transducer-immunoreceptor interphase is crucial for maintaining the analytical reliability of an assay. In this work, an overview of general approaches to the design of functional SPR-immunoassays is presented. It covers both immunosensors, the design of which utilizes well-known and often commercially available substrates, as well as the latest solutions developed in-house. Various approaches employing chemical and passive binding, affinity-based antibody immobilization, and the introduction of nanomaterial-based surfaces are discussed. The essence of their influence on the improvement of the main analytical parameters of a given immunosensor is explained. Particular attention is paid to solutions compatible with the latest trends in the development of label-free immunosensors, such as platforms dedicated to real-time monitoring in a quasi-continuous mode, the use of in situ-generated receptor layers (elimination of the regeneration step), and biosensors using recombinant and labelled protein receptors.

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“…Other authors effectively used SPR to measure the concentration of IgG. The receptor changed from a hen egg lysozyme [71] to recombinant staphylococcal protein A [72,73]. Protein A was also used in a label-free photonic crystal biosensor for detecting IgG [74]; however, the promising results of protein A need to be validated in real samples.…”

Section: Optical Biosensorsmentioning

confidence: 99%

Biosensors for Detecting Lymphocytes and Immunoglobulins

et al. 2020

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Lymphocytes (B, T and natural killer cells) and immunoglobulins are essential for the adaptive immune response against external pathogens. Flow cytometry and enzyme-linked immunosorbent (ELISA) kits are the gold standards to detect immunoglobulins, B cells and T cells, whereas the impedance measurement is the most used technique for natural killer cells. For point-of-care, fast and low-cost devices, biosensors could be suitable for the reliable, stable and reproducible detection of immunoglobulins and lymphocytes. In the literature, such biosensors are commonly fabricated using antibodies, aptamers, proteins and nanomaterials, whereas electrochemical, optical and piezoelectric techniques are used for detection. This review describes how these measurement techniques and transducers can be used to fabricate biosensors for detecting lymphocytes and the total content of immunoglobulins. The various methods and configurations are reported, along with the advantages and current limitations.

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Surface Plasmon Resonance Investigations of Bioselective Element Based on the Recombinant Protein A for Immunoglobulin Detection

Cited by 11 publications

References 27 publications

High‐Affinity Antibody Detection with a Bivalent Circularized Peptide Containing Antibody‐Binding Domains

High‐Affinity Antibody Detection with a Bivalent Circularized Peptide Containing Antibody‐Binding Domains

Recent Advancements in Receptor Layer Engineering for Applications in SPR-Based Immunodiagnostics

Biosensors for Detecting Lymphocytes and Immunoglobulins

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