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Electrokinetic effect for molecular recognition: A label-free approach for real-time biosensing
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2016 (English)In: Biosensors & bioelectronics, ISSN 0956-5663, E-ISSN 1873-4235, Vol. 82, p. 55-63Article in journal (Refereed) Published
Abstract [en]

We present a simple and inexpensive method for label-free detection of biomolecules. The method monitors the changes in streaming current in a fused silica capillary as target biomolecules bind to immobilized receptors on the inner surface of the capillary. To validate the concept, we show detection and time response of different protein-ligand and protein-protein systems: biotin-avidin and biotin-streptavidin, barstar-dibarnase and Z domain-immunoglobulin G (IgG). We show that specific binding of these biomolecules can be reliably monitored using a very simple setup. Using sequential injections of various proteins at a diverse concentration range and as well as diluted human serum we further investigate the capacity of the proposed technique to perform specific target detection from a complex sample. We also investigate the time for the signal to reach equilibrium and its dependence on analyte concentration and demonstrate that the current setup can be used to detect biomolecules at a concentration as low as 100 pM without requiring any advanced device fabrication procedures. Finally, an analytical model based on diffusion theory has been presented to explain the dependence of the saturation time on the analyte concentration and capillary dimensions and how reducing length and inner diameter of the capillary is predicted to give faster detection and in practice also lower limit of detection.

Place, publisher, year, edition, pages
2016. Vol. 82, p. 55-63
Keyword [en]
Diffusion model, Electrokinetic effect, Human serum analysis, Immunosensor, Label-free detection, Real-time biodetection, Bins, Biomolecules, Body fluids, Coenzymes, Electrodynamics, Fused silica, Immunosensors, Biodetection, Human serum, Proteins, avidin, barnase, immunoglobulin G, streptavidin, trastuzumab, Bacillus amyloliquefaciens ribonuclease, bacterial protein, barstar protein, Bacillus amyloliquefaciens, biotin, ligand, protein, ribonuclease, staphylococcus protein A, analytic method, Article, binding affinity, chemical procedures, concentration (parameters), genetic procedures, human, immobilization, limit of detection, microfluidics, molecular interaction, physical chemistry, physical parameters, process design, protein interaction, reaction time, zeta potential, Bacillus amyloliquefaciens, chemistry, devices, enzymology, equipment design, Staphylococcus aureus, Streptomyces, Bacterial Proteins, Biosensing Techniques, Humans, Ligands, Ribonucleases, Staphylococcal Protein A
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Computer and Information Sciences
Identifiers
URN: urn:nbn:se:ri:diva-32573DOI: 10.1016/j.bios.2016.03.060Scopus ID: 2-s2.0-84961718319OAI: oai:DiVA.org:ri-32573DiVA: diva2:1155605
Available from: 2017-11-08 Created: 2017-11-08 Last updated: 2018-01-13Bibliographically approved

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