Mixed Zwitterion-Based Self-Assembled Monolayer Interface for Impedimetric Glycomic Analyses of Human IgG Samples in an Array Format
| Autor: | Alica Vikartovská, Jan Krejčí, Lenka Lorencova, Tomas Bertok, Danica Mislovičová, Erika Dosekova, Alena Holazova, Darina Paprckova, Peter Kasak, Robert Plicka, Jan Tkac, Markéta Ilčíková, Stefan Belicky |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
rheumatoid arthritis
Glycosylation Diseases 02 engineering and technology Biosensing Techniques 01 natural sciences Covalent immobilization Arthritis Rheumatoid immunoglobulin G Protein Array Analysis Diagnosis Electrochemistry General Materials Science Spectroscopy Immunoassay medicine.diagnostic_test biology Chemistry Surfaces and Interfaces 021001 nanoscience & nanotechnology Condensed Matter Physics 3. Good health Body fluids plant lectin Bioanalytical methods Protein microarray Plant Lectins 0210 nano-technology devices Self assembled monolayers Glycan Chemical detection chemistry 010402 general chemistry Article Mixed self assembled monolayers blood Polysaccharides Monolayer medicine Humans human immunoassay procedures Detection of changes Diagnostic procedure Electrodes Monolayers Chromatography Proteins Lectin Self-assembled monolayer electrode 0104 chemical sciences Ricinus communis agglutinin-1 Biosensors protein microarray polysaccharide Immunoglobulin G biology.protein Lectin microarrays Gold Non-specific interactions genetic procedures Biosensor |
| Popis: | An impedimetric lectin biosensor for the detection of changes in the glycan structure of antibodies isolated from human serum is here correlated with the progression of rheumatoid arthritis (RA). The biosensor was built up from a mixed self-assembled monolayer (SAM) on gold consisting of two different thiolated zwitterionic derivatives, carboxybetaine and sulfobetaine, to resist nonspecific interactions. The carboxyl-terminated one was applied also for the covalent immobilization of lectin Ricinus communis agglutinin I (RCA-I). The process of building a bioreceptive layer was optimized and characterized using a diverse range of techniques. Impedimetric assays were integrated on a chip consisting of eight gold working electrodes, which is an important step toward the achievement of a moderate level of multiplexing for the analysis of human serum samples. At the end, the results obtained by the impedimetric analysis of immunoglobulins G (IgGs) isolated from serum samples were compared with those of two other standard bioanalytical methods employing lectins, that is, lectin microarrays (MAs) and enzyme-linked lectin binding assays (ELLBAs). The impedimetric results agreed very well with the DAS28 index (RA disease activity score 28), suggesting that impedimetric assays could be used for the development of a new diagnostic procedure sensitive to glycosylation changes in human IgGs and thus RA progression. 2016 American Chemical Society. Scopus |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|