Special Issue "Affinity Sensors"

A special issue of Biosensors (ISSN 2079-6374).

Deadline for manuscript submissions: closed (31 December 2015)

Special Issue Editors

Guest Editor
Prof. Dr. Nicole Jaffrezic-Renault

Institute of Analytical Sciences, UMR CNRS 5280, Department LSA, 5 Rue de La Doua, 69100 Villeurbanne, France
Website | E-Mail
Phone: +33472448306
Fax: +33 472 43 12 06
Interests: biosensors; impedance; immunosensors; conductometric sensors; enzymatic sensors; affinity sensors
Guest Editor
Dr. Carole Chaix

Département Laboratoire des Sciences Analytiques, Institut des Sciences Analytiques, UMR 5280 CNRS Université de Lyon, Université Lyon 1, Villeurbanne, 69100, France
E-Mail
Interests: electrochemical sensor; bioconjugation; oligonucleotide synthesis; click reaction; DNA sensor; methylene blue; ferrocene; nanomaterials; aptamer

Special Issue Information

Dear Colleagues,

This special issue of Biosensors will be devoted to Affinity Sensors. The special issue will consider innovative research and development on analytical devices which are based on affinity reactions and which integrate a biological material (e.g., tissue, microorganisms, organelles, cell receptors, antibodies, nucleic acids, natural products, etc.), a biologically derived material (e.g., recombinant antibodies, engineered proteins, aptamers, etc.) or a biomimic analogue (e.g., synthetic receptors, biomimetic catalysts, combinatorial ligands, imprinted polymers, etc.) intimately associated with or integrated within a physicochemical transducer or transducing microsystem, which may be optical, electrochemical, thermometric, piezoelectric, magnetic or micromechanical. Here, the focus is on the complementary intersection between molecular recognition, nanotechnology and supramolecular chemistry to improve the analytical performance and robustness of devices. All types of application domains are acceptable.

Prof. Dr. Nicole Jaffrezic-Renault
Dr. Carole Chaix
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biosensors is an international peer-reviewed open access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 350 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • affinity binding event
  • biomolecular interaction
  • biosensing
  • immunosensing
  • real-time monitoring
  • bio-functionalization
  • interface
  • nanomaterials
  • cell targeting
  • aptamer
  • DNA
  • transduction
  • electrochemical detection
  • SPR
  • sensitivity
  • specificity

Published Papers (5 papers)

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Research

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Open AccessArticle Protein-Flavonoid Interaction Studies by a Taylor Dispersion Surface Plasmon Resonance (SPR) Technique: A Novel Method to Assess Biomolecular Interactions
Biosensors 2016, 6(1), 6; doi:10.3390/bios6010006
Received: 17 December 2015 / Revised: 10 February 2016 / Accepted: 19 February 2016 / Published: 25 February 2016
Cited by 1 | PDF Full-text (1782 KB) | HTML Full-text | XML Full-text
Abstract
Flavonoids are common polyphenolic compounds widely distributed in fruits and vegetables. These pigments have important pharmacological relevance because emerging research suggests possible anti-cancer and anti-inflammatory properties as well other beneficial health effects. These compounds are relatively hydrophobic molecules, suggesting the role of blood
[...] Read more.
Flavonoids are common polyphenolic compounds widely distributed in fruits and vegetables. These pigments have important pharmacological relevance because emerging research suggests possible anti-cancer and anti-inflammatory properties as well other beneficial health effects. These compounds are relatively hydrophobic molecules, suggesting the role of blood transport proteins in their delivery to tissues. In this study, we assess the binding interactions of four flavonoids (kaempferol, luteolin, quercetin, and resveratrol) with human serum albumin (HSA), the most abundant protein in the blood, and with glutathione S-transferase pi isoform-1 (GSTP1), an enzyme with well-characterized hydrophobic binding sites that plays an important role in detoxification of xenobiotics with reduced glutathione, using a novel Taylor dispersion surface plasmon resonance (SPR) technique. For the first time, HSA sites revealed a high-affinity binding site for flavonoid interactions. Out of the four flavonoids that we examined, quercetin and kaempferol showed the strongest equilibrium binding affinities (KD) of 63 ± 0.03 nM and 37 ± 0.07 nM, respectively. GSTP1 displayed lower affinities in the micromolar range towards all of the flavonoids tested. The interactions of flavonoids with HSA and GSTP1 were studied successfully using this novel SPR assay method. The new method is compatible with both kinetic and equilibrium analyses. Full article
(This article belongs to the Special Issue Affinity Sensors)
Open AccessArticle A Label-Free Impedance Immunosensor Using Screen-Printed Interdigitated Electrodes and Magnetic Nanobeads for the Detection of E. coli O157:H7
Biosensors 2015, 5(4), 791-803; doi:10.3390/bios5040791
Received: 15 October 2015 / Revised: 5 December 2015 / Accepted: 11 December 2015 / Published: 15 December 2015
Cited by 8 | PDF Full-text (528 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Escherichia coli O157:H7 is one of the leading bacterial pathogens causing foodborne illness. In this study, an impedance immunosensor based on the use of magnetic nanobeads and screen-printed interdigitated electrodes was developed for the rapid detection of E. coli O157:H7. Magnetic nanobeads coated
[...] Read more.
Escherichia coli O157:H7 is one of the leading bacterial pathogens causing foodborne illness. In this study, an impedance immunosensor based on the use of magnetic nanobeads and screen-printed interdigitated electrodes was developed for the rapid detection of E. coli O157:H7. Magnetic nanobeads coated with anti-E. coli antibody were mixed with an E. coli sample and used to isolate and concentrate the bacterial cells. The sample was suspended in redox probe solution and placed onto a screen-printed interdigitated electrode. A magnetic field was applied to concentrate the cells on the surface of the electrode and the impedance was measured. The impedance immunosensor could detect E. coli O157:H7 at a concentration of 104.45 cfu·mL−1 (~1400 bacterial cells in the applied volume of 25 μL) in less than 1 h without pre-enrichment. A linear relationship between bacteria concentration and impedance value was obtained between 104 cfu·mL−1 and 107 cfu·mL−1. Though impedance measurement was carried out in the presence of a redox probe, analysis of the equivalent circuit model showed that the impedance change was primarily due to two elements: Double layer capacitance and resistance due to electrode surface roughness. The magnetic field and impedance were simulated using COMSOL Multiphysics software. Full article
(This article belongs to the Special Issue Affinity Sensors)
Figures

Open AccessArticle SPR Biosensor Probing the Interactions between TIMP-3 and Heparin/GAGs
Biosensors 2015, 5(3), 500-512; doi:10.3390/bios5030500
Received: 29 April 2015 / Revised: 8 July 2015 / Accepted: 10 July 2015 / Published: 23 July 2015
Cited by 5 | PDF Full-text (631 KB) | HTML Full-text | XML Full-text
Abstract
Tissue inhibitor of metalloproteinases-3 (TIMP-3) belongs to a family of proteins that regulate the activity of matrix metalloproteinases (MMPs), which can process various bioactive molecules such as cell surface receptors, chemokines, and cytokines. Glycosaminoglycans (GAGs) interact with a number of proteins, thereby playing
[...] Read more.
Tissue inhibitor of metalloproteinases-3 (TIMP-3) belongs to a family of proteins that regulate the activity of matrix metalloproteinases (MMPs), which can process various bioactive molecules such as cell surface receptors, chemokines, and cytokines. Glycosaminoglycans (GAGs) interact with a number of proteins, thereby playing an essential role in the regulation of many physiological/patho-physiological processes. Both GAGs and TIMP/MMPs play a major role in many cell biological processes, including cell proliferation, migration, differentiation, angiogenesis, apoptosis, and host defense. In this report, a heparin biosensor was used to map the interaction between TIMP-3 and heparin and other GAGs by surface plasmon resonance spectroscopy. These studies show that TIMP-3 is a heparin-binding protein with an affinity of ~59 nM. Competition surface plasmon resonance analysis indicates that the interaction between TIMP-3 and heparin is chain-length dependent, and N-sulfo and 6-O-sulfo groups (rather than the 2-O-sulfo groups) in heparin are important in the interaction of heparin with TIMP-3. Other GAGs (including chondroitin sulfate (CS) type E (CS-E)and CS type B (CS-B)demonstrated strong binding to TIMP-3, while heparan sulfate (HS), CS type A (CSA), CS type C (CSC), and CS type D (CSD) displayed only weak binding affinity. Full article
(This article belongs to the Special Issue Affinity Sensors)
Open AccessArticle Surface Plasmon Resonance (SPR) for the Evaluation of Shear-Force-Dependent Bacterial Adhesion
Biosensors 2015, 5(2), 276-287; doi:10.3390/bios5020276
Received: 30 April 2015 / Accepted: 19 May 2015 / Published: 26 May 2015
Cited by 7 | PDF Full-text (521 KB) | HTML Full-text | XML Full-text
Abstract
The colonization of Escherichia coli (E. coli) to host cell surfaces is known to be a glycan-specific process that can be modulated by shear stress. In this work we investigate whether flow rate changes in microchannels integrated on surface plasmon resonance
[...] Read more.
The colonization of Escherichia coli (E. coli) to host cell surfaces is known to be a glycan-specific process that can be modulated by shear stress. In this work we investigate whether flow rate changes in microchannels integrated on surface plasmon resonance (SPR) surfaces would allow for investigating such processes in an easy and high-throughput manner. We demonstrate that adhesion of uropathogenic E. coli UTI89 on heptyl α-d-mannopyranoside-modified gold SPR substrates is minimal under almost static conditions (flow rates of 10 µL·min−1), and reaches a maximum at flow rates of 30 µL·min−1 (≈30 mPa). This concept is applicable to the investigation of any ligand-pathogen interactions, offering a robust, easy, and fast method for screening adhesion characteristics of pathogens to ligand-modified interfaces. Full article
(This article belongs to the Special Issue Affinity Sensors)

Review

Jump to: Research

Open AccessReview Comparison of Electrochemical Immunosensors and Aptasensors for Detection of Small Organic Molecules in Environment, Food Safety, Clinical and Public Security
Biosensors 2016, 6(1), 7; doi:10.3390/bios6010007
Received: 22 December 2015 / Revised: 16 February 2016 / Accepted: 19 February 2016 / Published: 29 February 2016
Cited by 5 | PDF Full-text (2979 KB) | HTML Full-text | XML Full-text
Abstract
We review here the most frequently reported targets among the electrochemical immunosensors and aptasensors: antibiotics, bisphenol A, cocaine, ochratoxin A and estradiol. In each case, the immobilization procedures are described as well as the transduction schemes and the limits of detection. It is
[...] Read more.
We review here the most frequently reported targets among the electrochemical immunosensors and aptasensors: antibiotics, bisphenol A, cocaine, ochratoxin A and estradiol. In each case, the immobilization procedures are described as well as the transduction schemes and the limits of detection. It is shown that limits of detections are generally two to three orders of magnitude lower for immunosensors than for aptasensors, due to the highest affinities of antibodies. No significant progresses have been made to improve these affinities, but transduction schemes were improved instead, which lead to a regular improvement of the limit of detections corresponding to ca. five orders of magnitude over these last 10 years. These progresses depend on the target, however. Full article
(This article belongs to the Special Issue Affinity Sensors)

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