The effects of detergent on the enzyme-linked immunosorbent assay (ELISA) of blood group substances

McCabe, James; Fletcher, S.M.; Jones, Malcolm N.

doi:10.1016/0022-1759(88)90411-5

Cited by 22 publications

(7 citation statements)

References 16 publications

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“…11 Although promising, such sensitive force measurements required the use of a noncommercial AFM system. 11 Surfactants have been widely employed in traditional immunoassay formats, including radiolabeling, 12 solidphase immunofiltration, 13 and enzyme-linked immunosorbent assays, [14][15][16] to reduce background signal caused by nonspecific protein-protein adsorption. 12,[16][17][18][19] Prior work suggests that nonspecific adsorption of proteinaceous material via primarily hydrophobic interactions is greatly reduced using nonionic surfactants.…”

Section: Introductionmentioning

confidence: 99%

“…Surfactants have been widely employed in traditional immunoassay formats, including radiolabeling, solid-phase immunofiltration, and enzyme-linked immunosorbent assays, − to reduce background signal caused by nonspecific protein−protein adsorption. ,− Prior work suggests that nonspecific adsorption of proteinaceous material via primarily hydrophobic interactions is greatly reduced using nonionic surfactants . Indeed, several groups have reported that the addition of Tween 20, Triton X-100, and Tween 80 to antibody−antigen precipitation studies greatly reduced nonspecific adhesion. ,,− Such surfactants have also been shown to reduce nonspecific protein−protein interactions in other immunoassay formats.…”

Section: Introductionmentioning

confidence: 99%

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Influence of Surfactants and Antibody Immobilization Strategy on Reducing Nonspecific Protein Interactions for Molecular Recognition Force Microscopy

Brogan

Shin

2004

Langmuir

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Specific and nonspecific interactions between antibody-modified probes and substrate-immobilized proteins were monitored by atomic force microscopy (AFM). Probes were modified with anti-ovalbumin IgG antibodies immobilized in either an oriented or a random manner. The oriented immobilization of whole IgG was accomplished through the use of Protein A, and random immobilization was carried out with glutaraldehyde. Nonspecific interactions may lead to false detection of antibody-antigen binding events even when the antigen binding sites are properly positioned by an oriented immobilization strategy. Thus, nonionic and zwitterionic surfactants, including Tween 20, Tween 80, Triton X-100, and CHAPS, were evaluated to determine if nonspecific binding events could be reduced without compromising the desired specific antibody-antigen binding. Enzyme-linked immunosorbent assay and surface plasmon resonance assays were also employed to study antibody-antigen binding as a function of immobilization strategy and surfactant concentration. The data from these studies indicate that Protein A can be used to immobilize whole IgG onto AFM probes for force measurement experiments and that a surfactant is useful for improving the selectivity for such measurements.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Influence of Surfactants and Antibody Immobilization Strategy on Reducing Nonspecific Protein Interactions for Molecular Recognition Force Microscopy

Brogan

Shin

2004

Langmuir

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“…For example, high concentrations of detergent, which are often used in harvesting protein from cells, can lead to displacement of adsorbed antigen probes from assay surfaces, e.g., ELISA. 68 Con-sequently, the interrogation of biological samples containing detergents could disrupt assay sensitivity by affecting the stability of noncovalently bound SBPs on the sensor surface. Such noncovalent functionalization, however, could also allow facile regeneration of the sensor surface, whereby the sensor can be reused repeatedly after stripping the spent biofunctional layer.…”

Section: ■ Discussionmentioning

confidence: 99%

Chimeric Peptide-Based Biomolecular Constructs for Versatile Nucleic Acid Biosensing

Lee

Zareie

Sarıkaya

2022

ACS Appl. Mater. Interfaces

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Nucleic acid biomarkers hold great potential as key indicators for the diagnosis and monitoring of diseases. Herein we design and implement bifunctional chimeric biomolecules composed of a solid-binding peptide (SBP) domain that specifically adsorbs onto solid sensor surfaces and a peptide nucleic acid (PNA) moiety that facilitates anchoring of antisense oligonucleotide (ASO) probes for the detection of nucleic acid targets. A gold-binding peptide, AuBP1, previously selected by directed evolution to specifically bind to gold, served as the basis for immobilizing nucleic acid probes onto gold substrates. Using surface plasmon resonance (SPR) spectroscopy and quartz crystal microbalance (QCM) analyses, we demonstrate the sequential biomolecular assembly of the heterofunctional solid-binding peptide–antisense oligomer (SBP-ASO) construct onto a sensor surface and the subsequent detection of DNA in an aqueous environment. The effect of steric hindrance on optimal probe assembly is observed, establishing that less packing density results in greater target capture efficacy. In addition, an adsorbed layer of chimeric solid-binding peptide–peptide nucleic acid (SBP-PNA) undergoes viscoelastic changes at the solid–liquid interface upon probe immobilization and DNA target capture, whereby the rigid biofunctional layer becomes more flexible. The dual nature of the chimeric construct is highly amenable to a variety of platforms allowing for both specific recognition and probe immobilization on the sensor surface, while the modular design of the solid-binding peptide–antisense oligonucleotide provides facile functionalization of a wide diversity of solid substrates.

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“…Although the stability of the antigen was an initial problem, SDS denaturation of the purified rRCT rendered the antigen stable over time and temperatures and did not affect antibody binding to the non-conformationally dependent epitope. As long as the SDS concentration is kept below its critical micelle concentration, it has been shown to improve ELISA responses in other systems (15). Bacterial lysate containing rRAP-1 from B. caballi is similarly heat sensitive but also is stabilized in the presence of SDS (8).…”

Section: Discussionmentioning

confidence: 99%

Competitive Enzyme-Linked Immunosorbent Assay Based on a Rhoptry-Associated Protein 1 Epitope Specifically Identifies Babesia bovis -Infected Cattle

Goff

McElwain

Suárez

et al. 2003

Clin Vaccine Immunol

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The competitive enzyme-linked immunosorbent assay (cELISA) format has proven to be an accurate, reliable, easily standardized, and high-throughput method for detecting hemoparasite infections. In the present study, a species-specific, broadly conserved, and tandemly repeated B-cell epitope within the C terminus of the rhoptry-associated protein 1 of the hemoparasite Babesia bovis was cloned and expressed as a histidine-tagged thioredoxin fusion peptide and used as antigen in a cELISA. The assay was optimized with defined negative and positive bovine sera, where positive sera inhibited the binding of the epitope-specific monoclonal antibody BABB75A4. The cELISA accurately differentiated animals with B. bovis-specific antibodies from uninfected animals and from animals with antibodies against other tick-borne hemoparasites (98.7% specificity). In addition, B. bovis-specific sera from Australia, Argentina, Bolivia, Puerto Rico, and Morocco inhibited the binding of BABB75A4, confirming conservation of the epitope. The assay first detected experimentally infected animals between 13 and 17 days postinfection, and with sera from naturally infected carrier cattle, was comparable to indirect immunofluorescence (98.3% concordance). The assay appears to have the characteristics necessary for an epidemiologic and disease surveillance tool.

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The effects of detergent on the enzyme-linked immunosorbent assay (ELISA) of blood group substances

Cited by 22 publications

References 16 publications

Influence of Surfactants and Antibody Immobilization Strategy on Reducing Nonspecific Protein Interactions for Molecular Recognition Force Microscopy

Influence of Surfactants and Antibody Immobilization Strategy on Reducing Nonspecific Protein Interactions for Molecular Recognition Force Microscopy

Chimeric Peptide-Based Biomolecular Constructs for Versatile Nucleic Acid Biosensing

Competitive Enzyme-Linked Immunosorbent Assay Based on a Rhoptry-Associated Protein 1 Epitope Specifically Identifies Babesia bovis -Infected Cattle

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