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Biosensors, Volume 4, Issue 3 (September 2014) – 8 articles , Pages 189-328

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346 KiB  
Communication
Microelectrode Arrays and the Use of PEG-Functionalized Diblock Copolymer Coatings
by Sakshi Uppal, Matthew D. Graaf and Kevin D. Moeller
Biosensors 2014, 4(3), 318-328; https://doi.org/10.3390/bios4030318 - 11 Sep 2014
Cited by 10 | Viewed by 6454
Abstract
PEG-modified diblock copolymer surfaces have been examined for their compatibility with microelectrode array based analytical methods. The use of PEG-modified polymer surfaces on the arrays was initially problematic because the redox couples used in the experiments were adsorbed by the polymer. This led [...] Read more.
PEG-modified diblock copolymer surfaces have been examined for their compatibility with microelectrode array based analytical methods. The use of PEG-modified polymer surfaces on the arrays was initially problematic because the redox couples used in the experiments were adsorbed by the polymer. This led the current measured by cyclic voltammetry for the redox couple to be unstable and increase with time. However, two key findings allow the experiments to be successful. First, after multiple cyclic voltammograms the current associated with the redox couple does stabilize so that a good baseline current can be established. Second, the rate at which the current stabilizes is consistent every time a particular coated array is used. Hence, multiple analytical experiments can be conducted on an array coated with a PEG-modified diblock copolymer and the data obtained is comparable as long as the data for each experiment is collected at a consistent time point. Full article
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<p>Diblock copolymer for coating arrays.</p>
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<p>CV for FCA on a microelectrode array (scans 20–40).</p>
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<p>Red line—CV for FCA with the PEG functionalized polymer coating. Black line —CV for FCA with the unfunctionalized polymer.</p>
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<p>Curve for the nonspecific binding of BSA to an array coated with a PEG functionalized polymer.</p>
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<p>Binding curves generated at different time points.</p>
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<p>Comparison of polymers functionalized with different lengths of PEG.</p>
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<p>Chan-Lam type coupling reaction on a microelectrode array.</p>
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454 KiB  
Review
Piezoelectric Biosensors for Organophosphate and Carbamate Pesticides: A Review
by Giovanna Marrazza
Biosensors 2014, 4(3), 301-317; https://doi.org/10.3390/bios4030301 - 9 Sep 2014
Cited by 110 | Viewed by 16354
Abstract
Due to the great amount of pesticides currently being used, there is an increased interest for developing biosensors for their detection. Among all the physical transducers, piezoelectric systems have emerged as the most attractive due to their simplicity, low instrumentation costs, possibility for [...] Read more.
Due to the great amount of pesticides currently being used, there is an increased interest for developing biosensors for their detection. Among all the physical transducers, piezoelectric systems have emerged as the most attractive due to their simplicity, low instrumentation costs, possibility for real-time and label-free detection and generally high sensitivity. This paper presents an overview of biosensors based on the quartz crystal microbalance, which have been reported in the literature for organophosphate and carbamate pesticide analysis. Full article
(This article belongs to the Special Issue Piezoelectric Biosensors)
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<p>Chemical structure of Organophosphates.</p>
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<p>Chemical structure of Carbamates.</p>
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<p>Schematic of a piezoelectric quartz crystal.</p>
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<p>Schematic electrochemical quartz crystal microbalance (EQCM) apparatus.</p>
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<p>Scheme of the relation between action on sensor surface and resulting frequency <span class="html-italic">versus</span> time curve, showing an antibody–antigen reaction as an example.</p>
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<p>(<b>a</b>) Adsorption immobilization scheme. (<b>b</b>) General route for covalent immobilization of bioreceptors.</p>
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1297 KiB  
Review
Biosensors with Built-In Biomolecular Logic Gates for Practical Applications
by Yu-Hsuan Lai, Sin-Cih Sun and Min-Chieh Chuang
Biosensors 2014, 4(3), 273-300; https://doi.org/10.3390/bios4030273 - 27 Aug 2014
Cited by 38 | Viewed by 10944
Abstract
Molecular logic gates, designs constructed with biological and chemical molecules, have emerged as an alternative computing approach to silicon-based logic operations. These molecular computers are capable of receiving and integrating multiple stimuli of biochemical significance to generate a definitive output, opening a new [...] Read more.
Molecular logic gates, designs constructed with biological and chemical molecules, have emerged as an alternative computing approach to silicon-based logic operations. These molecular computers are capable of receiving and integrating multiple stimuli of biochemical significance to generate a definitive output, opening a new research avenue to advanced diagnostics and therapeutics which demand handling of complex factors and precise control. In molecularly gated devices, Boolean logic computations can be activated by specific inputs and accurately processed via bio-recognition, bio-catalysis, and selective chemical reactions. In this review, we survey recent advances of the molecular logic approaches to practical applications of biosensors, including designs constructed with proteins, enzymes, nucleic acids, nanomaterials, and organic compounds, as well as the research avenues for future development of digitally operating “sense and act” schemes that logically process biochemical signals through networked circuits to implement intelligent control systems. Full article
(This article belongs to the Special Issue Electrochemical and Biomedical Sensors)
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Figure 1
<p>Biocatalytic cascade used to perform a NOR logic operation for the assessment of distinct classes of threat agents [<a href="#B13-biosensors-04-00273" class="html-bibr">13</a>] (doi:10.1039/C0CC05716A). Reproduced with permission of The Royal Society of Chemistry.</p>
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<p>Illustrative diagram of the self-powered, biocomputing, logically-controlled “sense-act-treat” system based on a biofuel cell. Reprinted from [<a href="#B20-biosensors-04-00273" class="html-bibr">20</a>] with permission of John Wiley and Sons. Copyright © 2012 WILEY-VCH Verlag GmbH &amp; Co. KGaA, Weinheim.</p>
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<p>Schematic diagram of a translator AND gate incorporating miR-21 and miR-122 as inputs with resulting fluorescent output. Reprinted with permission from [<a href="#B27-biosensors-04-00273" class="html-bibr">27</a>]. Copyright © 2013, American Chemical Society.</p>
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<p>Integration of YES and OR logic gates based on the combination of two molecular beacons and DNA motifs for detection of Mtb and its resistance to Rif. Reproduced from [<a href="#B31-biosensors-04-00273" class="html-bibr">31</a>] with permission of John Wiley and Sons. Copyright © 2012 WILEY-VCH Verlag GmbH &amp; Co. KGaA, Weinheim.</p>
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<p>The strip “OR” logical gate using thrombin and ATP as inputs. SA: streptavidin, TZ: test zone, CZ: control zone. Reprinted with permission from [<a href="#B39-biosensors-04-00273" class="html-bibr">39</a>]. Copyright © 2012, American Chemical Society.</p>
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<p>Schematic illustration of DNAzyme-involved (<b>A</b>) AND and (<b>B</b>) ANDNOT gate operations upon presence of their inputs. Reprinted with permission from [<a href="#B50-biosensors-04-00273" class="html-bibr">50</a>]. Copyright © 2013, Rights Managed by Nature Publishing Group.</p>
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<p>Design of aptamer-gated DNA nanorobot. (<b>A</b>) Schematic front view of closed nanorobot loaded with proteins. (<b>B</b>) The aptamer lock mechanism. (<b>C</b>) A nanorobot opened by ligand displacement of aptamer locks. From [<a href="#B54-biosensors-04-00273" class="html-bibr">54</a>], reprinted with permission from AAAS.</p>
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<p>Schematic detection of (<b>A</b>) both a protein and a nucleic acid sequence as well as (<b>B</b>) only a protein. Reprinted with permission from [<a href="#B56-biosensors-04-00273" class="html-bibr">56</a>]. Copyright © 2009, American Chemical Society.</p>
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<p>Biomolecular logical gate strategy for the detection of NDM-1-specific nucleic acids and its drug-resistance activity. [<a href="#B59-biosensors-04-00273" class="html-bibr">59</a>]—Reproduced by permission of The Royal Society of Chemistry (doi:10.1039/c4cc01108b).</p>
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<p>The design for simultaneous detection of H<sub>2</sub>O<sub>2</sub> and caspase 8 activity through chemical reactions releasing Hydroxy-cyanobenzothiazole and D-cysteine and <span class="html-italic">in situ</span> formation of firefly luciferin. Reprinted with permission from [<a href="#B63-biosensors-04-00273" class="html-bibr">63</a>]. Copyright © 2013, American Chemical Society.</p>
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<p>The <b>AND</b> logical cellular sensor sensitive to arsenic and mercury ions. Reproduced from [<a href="#B65-biosensors-04-00273" class="html-bibr">65</a>] © 2012 Elsevier B.V. All rights reserved. Under the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).</p>
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1487 KiB  
Article
Study of Paclitaxel-Treated HeLa Cells by Differential Electrical Impedance Flow Cytometry
by Julie Kirkegaard, Casper Hyttel Clausen, Romen Rodriguez-Trujillo and Winnie Edith Svendsen
Biosensors 2014, 4(3), 257-272; https://doi.org/10.3390/bios4030257 - 13 Aug 2014
Cited by 24 | Viewed by 9461
Abstract
This work describes the electrical investigation of paclitaxel-treated HeLa cells using a custom-made microfluidic biosensor for whole cell analysis in continuous flow. We apply the method of differential electrical impedance spectroscopy to treated HeLa cells in order to elucidate the changes in electrical [...] Read more.
This work describes the electrical investigation of paclitaxel-treated HeLa cells using a custom-made microfluidic biosensor for whole cell analysis in continuous flow. We apply the method of differential electrical impedance spectroscopy to treated HeLa cells in order to elucidate the changes in electrical properties compared with non-treated cells. We found that our microfluidic system was able to distinguish between treated and non-treated cells. Furthermore, we utilize a model for electrical impedance spectroscopy in order to perform a theoretical study to clarify our results. This study focuses on investigating the changes in the electrical properties of the cell membrane caused by the effect of paclitaxel. We observe good agreement between the model and the obtained results. This establishes the proof-of-concept for the application in cell drug therapy. Full article
(This article belongs to the Special Issue Label-Free Biosensors: Exploring the Field)
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Figure 1
<p>Schematic drawing of the setup. A multi-frequency lock-in amplifier is used to generate a signal and to detect the impedance. The signal generated between the electrodes in the channel is passed through a current trans-amplifier before it is returned to the lock-in amplifier. The detection unit consists of a microfluidic channel with expansions around the electrodes in order to decrease the overall impedance of the system, thus improving signal quality. The sample is pumped through the channel, and cells perturb the electrical impedance as they pass over the electrodes. Differential impedance between the two measuring electrodes is recorded for further analysis. The figure is not drawn to scale.</p>
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<p>Schematic drawing of the equivalent circuit model.</p>
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<p>Calculated opacity response of a bead, an intact cell and cells with varying electrical properties of the membrane based on the MMT model. The values changed are 1/<span class="html-italic">σ<sub>mem</sub></span> and ε<span class="html-italic"><sub>mem</sub></span>. The vertical line represents the high frequency used in this work to investigate the paclitaxel-treated and non-treated HeLa cells. The low frequency used is 82 kHz.</p>
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<p>Data analysis of the impedance response of 4.5- and 10-µm beads. The measurements were normalized to one for comparison; the frequencies used were high frequency (HF) at 1.57 MHz and low frequency (LF) at 82 kHz. (<b>A</b>) Maximum differential impedance scatter plot of the opacity response as a function of the LF impedance. (<b>B</b>) Histogram distribution of the LF impedance. (<b>C</b>) Histogram distribution of the opacity.</p>
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<p>Data analysis of the impedance response of treated and non-treated cells; the frequencies used were HF at 1.57 MHz and LF at 82 kHz. (<b>A</b>) Maximum differential impedance scatter plot of the opacity response as a function of the LF impedance signal of the three different samples, where the bead data has been removed (see the <a href="#app1-biosensors-04-00257" class="html-app">Appendix</a>). (<b>B</b>) Histogram distribution of the LF impedance signal. (<b>C</b>) Histogram distribution of the opacity of the different samples; beads and treated cells, beads and non-treated cells and beads plus treated and non-treated cells.</p>
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<p>Optical image of the used cell sample with a 50/50 mix of treated and non-treated cells stained with trypan blue (scale bar: 50 µm). The red and green arrows are alive and dead cells.</p>
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<p>Bode plot. Frequency sweep of an electrode set from one of the chips used in this study. The black vertical lines represent the values of the frequencies used in the study, 82 kHz, 210 kHz and 1.57 MHz.</p>
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<p>Scatter plot of amplitudes for LF = 82 kHz and HF = 1.57 MHz. The figure shows the opacity response as a function of the LF signal of three different sample mixtures; beads and treated cells, beads and non-treated cells and bead plus treated and non-treated cells. The 4.5-µm beads from the three sets are visible in the top left corner centered on one.</p>
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<p>Data analysis of the impedance response of treated and non-treated cells; the frequencies used were high frequency (HF) at 1.57 MHz and low frequency (LF) at 210 kHz. (<b>A</b>) Histogram distribution of the opacity (HF/LF) of the different samples; beads and treated cells, beads and non-treated cells and bead plus treated and non-treated cells. (<b>B</b>) Amplitude scatter plot of the opacity response as a function of the LF signal of three different samples. (<b>C</b>) Optical image of the used cell sample with a 50/50 mix of treated and non-treated cells stained with trypan blue (scale bar: 50 µm). (<b>D</b>) Histogram distribution of the LF signal.</p>
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645 KiB  
Review
Electrochemical Biosensors Based on Ferroceneboronic Acid and Its Derivatives: A Review
by Baozhen Wang, Shigehiro Takahashi, Xiaoyan Du and Jun-ichi Anzai
Biosensors 2014, 4(3), 243-256; https://doi.org/10.3390/bios4030243 - 30 Jul 2014
Cited by 39 | Viewed by 9468
Abstract
We review recent progress in the development of electrochemical biosensors based on ferroceneboronic acid (FcBA) and ferrocene (Fc)-modified boronic acids. These compounds can be used to construct electrochemical biosensors because they consist of a binding site (i.e., a boronic acid moiety) [...] Read more.
We review recent progress in the development of electrochemical biosensors based on ferroceneboronic acid (FcBA) and ferrocene (Fc)-modified boronic acids. These compounds can be used to construct electrochemical biosensors because they consist of a binding site (i.e., a boronic acid moiety) and an electrochemically active part (i.e., an Fc residue). By taking advantage of the unique properties of FcBA and its derivatives, electrochemical sensors sensitive to sugars, glycated hemoglobin (HbA1c), fluoride (F) ions, and so forth have been widely studied. FcBA-based sugar sensors rely on the selective binding of FcBA to 1,2- or 1,3-diol residues of sugars through the formation of cyclic boronate ester bonds. The redox properties of FcBA-sugar adduct differ from those of free FcBA, which forms the basis of the electrochemical determination of sugars. Thus, non-enzymatic glucose sensors are now being actively studied using FcBA and Fc-modified boronic acids as redox markers. Using a similar principle, HbA1c can be detected by FcBA-based electrochemical systems because it contains hydrocarbon chains on the polypeptide chain. HbA1c sensors are useful for monitoring blood glucose levels over the preceding 8–12 weeks. In addition, FcBA and Fc-modified boronic acids have been used for the detection of F ions due to the selective binding of boronic acid to F ions. F-ion sensors may be useful alternatives to conventional ion-selective electrodes sensitive to F ion. Furthermore, FcBA derivatives have been studied to construct lectin; steroids; nucleotides; salicylic acid; and bacteria sensors. One of the limitations of FcBA-based sensors comes from the fact that FcBA derivatives are added in sample solutions as reagents. FcBA derivatives should be immobilized on the surface of electrodes for developing reagentless sensors. Full article
(This article belongs to the Special Issue Electrochemical and Biomedical Sensors)
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Figure 1
<p>Binding equilibria of phenylboronic acid to sugar and OH<sup>−</sup> ion.</p>
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<p>Chemical structures of ferroceneboronic acid and its derivatives.</p>
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<p>Cyclic voltammograms of 0.1 mM FcBA in the presence of (<b>a</b>) fructose and (<b>b</b>) glucose at pH 7.0. Scan rate: 50 mV·s<sup>−1</sup>. Reprinted with permission from Takahashi <span class="html-italic">et al</span>. [<a href="#B9-biosensors-04-00243" class="html-bibr">9</a>]. Copyright (2011) Elsevier.</p>
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<p>Changes in the reduction peak currents (I/I<sub>0</sub>) in CV of FcBA as a function of the concentration of phenolic compounds: (<b>a</b>) mandelic acid, (<b>b</b>) salicylamide, (<b>c</b>) 2-hydroxybenzylalcohol, (<b>d</b>) salicylic acid, and (<b>e</b>) salicylhydroxamic acid. Reprinted with permission from Takahashi <span class="html-italic">et al</span>. [<a href="#B9-biosensors-04-00243" class="html-bibr">9</a>]. Copyright (2011) Elsevier.</p>
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<p>Chemical structure of <span class="html-italic">N</span>,<span class="html-italic">N</span>-dimethylaminomethyl-substituted FcBA (<b>1</b>) and a schematic illustration of reaction of LPS sensing by enzyme-modified electrode. Reprinted with permission from Kato <span class="html-italic">et al</span>. [<a href="#B14-biosensors-04-00243" class="html-bibr">14</a>]. Copyright (2007) Elsevier.</p>
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<p>Chemical structure of Fc-substituted thiopheneboronic acid.</p>
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<p>Calibration graphs for HbA1c in samples containing different total concentrations of Hb. The voltammetric peak current was recorded for 3 μL sample solutions. Reprinted with permission from Scheller <span class="html-italic">et al</span>. [<a href="#B19-biosensors-04-00243" class="html-bibr">19</a>]. Copyright (2006) Elsevier.</p>
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<p>Amperometric response of FcBA to glucose and FV. The output current was recorded at 0.1 V <span class="html-italic">vs</span>. Ag/AgCl. 1 mM glucose (<b>a</b>,<b>b</b>) and 0.5 mM FV (<b>c</b>–<b>j</b>) were added to the sample solution. (Inset) A calibration graph for FV. Reprinted with permission from Chien <span class="html-italic">et al</span>. [<a href="#B24-biosensors-04-00243" class="html-bibr">24</a>]. Copyright (2011) Wiley-VCH Verlag GmbH &amp; Co.</p>
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<p>Chemical structure of catecholboryl-modified ferrocene.</p>
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<p>Chemical structures of ferrocene-modified benzoboroxoles.</p>
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824 KiB  
Review
Sensing Magnetic Directions in Birds: Radical Pair Processes Involving Cryptochrome
by Roswitha Wiltschko and Wolfgang Wiltschko
Biosensors 2014, 4(3), 221-242; https://doi.org/10.3390/bios4030221 - 24 Jul 2014
Cited by 69 | Viewed by 17412
Abstract
Birds can use the geomagnetic field for compass orientation. Behavioral experiments, mostly with migrating passerines, revealed three characteristics of the avian magnetic compass: (1) it works spontaneously only in a narrow functional window around the intensity of the ambient magnetic field, but can [...] Read more.
Birds can use the geomagnetic field for compass orientation. Behavioral experiments, mostly with migrating passerines, revealed three characteristics of the avian magnetic compass: (1) it works spontaneously only in a narrow functional window around the intensity of the ambient magnetic field, but can adapt to other intensities, (2) it is an “inclination compass”, not based on the polarity of the magnetic field, but the axial course of the field lines, and (3) it requires short-wavelength light from UV to 565 nm Green. The Radical Pair-Model of magnetoreception can explain these properties by proposing spin-chemical processes in photopigments as underlying mechanism. Applying radio frequency fields, a diagnostic tool for radical pair processes, supports an involvement of a radical pair mechanism in avian magnetoreception: added to the geomagnetic field, they disrupted orientation, presumably by interfering with the receptive processes. Cryptochromes have been suggested as receptor molecules. Cry1a is found in the eyes of birds, where it is located at the membranes of the disks in the outer segments of the UV-cones in chickens and robins. Immuno-histochemical studies show that it is activated by the wavelengths of light that allow magnetic compass orientation in birds. Full article
(This article belongs to the Special Issue Magnetic Biosensors)
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Graphical abstract
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<p>(<b>a</b>) Section through a frequently used test cage for recording the activity of a migratory bird [<a href="#B11-biosensors-04-00221" class="html-bibr">11</a>]. (<b>b</b>) Orientation of robins during spring migration (<b>left</b>) in the local geomagnetic field and (<b>right</b>) with magnetic North turned by 120° to ESE (data from [<a href="#B13-biosensors-04-00221" class="html-bibr">13</a>]). The triangles at the periphery of the circle mark the mean headings of individual birds, the arrow represents the grand mean vector based on these headings drawn proportional to the radius of the circle. The two inner circles indicate the 5% (dotted) and the 1% significance border of the Rayleigh test [<a href="#B14-biosensors-04-00221" class="html-bibr">14</a>].</p>
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<p>The functional window of the magnetic compass and its flexibility: orientation of robins in various magnetic intensities. Blue: +, oriented behavior; red: −, disoriented behavior. The dashed line marks the local intensity of the capture site, 46 μT. The blue zones indicate the estimated functional range of the magnetic compass in birds kept in the intensity indicated at the abscissa; the grey zone marks the intensity range presently found on Earth (data from [<a href="#B15-biosensors-04-00221" class="html-bibr">15</a>,<a href="#B17-biosensors-04-00221" class="html-bibr">17</a>,<a href="#B18-biosensors-04-00221" class="html-bibr">18</a>]).</p>
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<p>The avian inclination compass: cross-section through the magnetic field as seen from the West. N, S, geographic North and South; H, magnetic vector; He, vector of the local geomagnetic field; Hh, Hv. horizontal and vertical component of the magnetic field, with the red arrow tips indicating the polarity; the axial course of the field lines is indicated in blue. g, gravity vector indicating downward. Red »mN«, »mS«, <span class="html-italic">magnetic North</span> and <span class="html-italic">South</span>, the readings of a polarity compass; blue »p«, »e«, <span class="html-italic">poleward</span> and <span class="html-italic">equatorward</span>, the readings of the avian inclination compass. The robins’ flying direction indicates where the birds seek their spring migratory direction (after [<a href="#B19-biosensors-04-00221" class="html-bibr">19</a>], modified).</p>
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<p>Orientation of robins under narrow band-lights of various wavelengths. (<b>a</b>) Spectra of the test lights produced by light-emitting diodes. (<b>b</b>) Orientation behavior under the various lights, with the peak wavelength indicated in the figure. The light intensity was about 8 × 10<sup>15</sup> quanta/s·m<sup>2</sup>, except under UV, where it was only 0.8 × 10<sup>15</sup> quanta/s·m<sup>2</sup>.—Symbols as in <a href="#biosensors-04-00221-f001" class="html-fig">Figure 1</a>b (data from [<a href="#B25-biosensors-04-00221" class="html-bibr">25</a>,<a href="#B26-biosensors-04-00221" class="html-bibr">26</a>,<a href="#B29-biosensors-04-00221" class="html-bibr">29</a>,<a href="#B30-biosensors-04-00221" class="html-bibr">30</a>]).</p>
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<p>The Radical Pair Model of magnetoreception. (<b>a</b>) Scheme of the radical pair mechanisms proposed by Ritz and colleagues [<a href="#B35-biosensors-04-00221" class="html-bibr">35</a>]. After photon absorption, a radical pair is generated by an electron transfer from a donor (D) to an acceptor (A), with the ratio singlet/triplet depending on the alignment of the molecule in the external magnetic field. The red arrows represent the spins of the electrons. The changing singlet/triplet ratio as a function of the alignment is indicated in the inner diagram; note that 0° = 180° and 90° = 270°. The amount of singlet and triplet products is symbolized for a parallel alignment and a 40° alignment. (<b>b</b>) Light rays are projected onto the retina, activating receptor cells that are aligned at different angles with respect to the direction of the magnetic vector B (from [<a href="#B33-biosensors-04-00221" class="html-bibr">33</a>], modified).</p>
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<p>Testing robins with radio frequency fields of 7 MHz, 470 nT, added in different alignments with respect to the vector of the local geomagnetic field. (<b>a</b>) Control: geomagnetic field only; (<b>b</b>) radio frequency field added parallel to the magnetic vector, that is 24° to the downward direction; (<b>c</b>) added vertically, 24° to the magnetic vector; (<b>d</b>) added 48° to the magnetic vector, which means 24° to the downward direction—Symbols as in <a href="#biosensors-04-00221-f001" class="html-fig">Figure 1</a>b (data from [<a href="#B44-biosensors-04-00221" class="html-bibr">44</a>]).</p>
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<p>Summary of the tests with different frequencies and different intensities: (<b>a</b>) in the geomagnetic field of 46 μT and (<b>b</b>) in a 92 μT field, twice that intensity. Red: −, disoriented behavior, indicating an interference with magnetoreception; blue: + no disruptive effect of the respective oscillating field. Solid symbols: results from experiments, open symbols: inferred from the other results under the assumption of monotony (based on data from [<a href="#B48-biosensors-04-00221" class="html-bibr">48</a>]).</p>
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<p>Localization of cryptochrome 1a (Cry1a) in the retina of robins and chickens. (<b>a</b>) Immuno-labeling of Cry1a and UV-opsin and their co-localization in the retina of robins. A, Vertical section through the outer part of retina; B, whole mount of a retina. (<b>b</b>) Electron-microscopic images of the outer segments of the UV/V-cones, with labeled Cry1a visible as dark dots along the disk membranes. A, entire outer segment of a chicken V-cone. B, higher magnification of the lower part of this outer segment. C, Part of the outer segment of an UV-cone of a robin. (<b>c</b>) Western blots of robin (D) and chicken (E) retina showing Cry1a in the cytosol and membrane fraction. F1, cytosolic fraction; F2, membrane fraction; F3, nuclear fraction; F4, cytoskeletal fraction; T, tongue tissue as control (from [<a href="#B59-biosensors-04-00221" class="html-bibr">59</a>]).</p>
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<p>The amount of activated Cry1a, labeled with a specific antiserum, in the retina of chickens after illumination with light of various wavelengths. UV, 373 nm UV light; B, 424 nm blue light; T, 502 nm turquoise light; G, 565 nm green light; Y, 590 nm yellow light; R, 635 nm red light, see <a href="#biosensors-04-00221-f004" class="html-fig">Figure 4</a>a (from [<a href="#B77-biosensors-04-00221" class="html-bibr">77</a>]).</p>
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<p>The redox cycle of flavin. FADox, oxidized flavin; FADH<sup>●</sup>, photo-reduced neutral radical form; FADH<sup>−</sup>, fully reduced form. Nt, nitrogen-terminus; Ct, carboxy-terminus of the Cry1a, with the antiserum-binding epitope in red. In parentheses, radical pairs, black arrows indicate light-independent reactions (from [<a href="#B77-biosensors-04-00221" class="html-bibr">77</a>] after [<a href="#B79-biosensors-04-00221" class="html-bibr">79</a>], modified).</p>
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635 KiB  
Article
An Inexpensive, Fast and Sensitive Quantitative Lateral Flow Magneto-Immunoassay for Total Prostate Specific Antigen
by Jacqueline M. Barnett, Patrick Wraith, Janice Kiely, Raj Persad, Katrina Hurley, Peter Hawkins and Richard Luxton
Biosensors 2014, 4(3), 204-220; https://doi.org/10.3390/bios4030204 - 8 Jul 2014
Cited by 48 | Viewed by 10244
Abstract
We describe the detection characteristics of a device the Resonant Coil Magnetometer (RCM) to quantify paramagnetic particles (PMPs) in immunochromatographic (lateral flow) assays. Lateral flow assays were developed using PMPs for the measurement of total prostate specific antigen (PSA) in serum samples. A [...] Read more.
We describe the detection characteristics of a device the Resonant Coil Magnetometer (RCM) to quantify paramagnetic particles (PMPs) in immunochromatographic (lateral flow) assays. Lateral flow assays were developed using PMPs for the measurement of total prostate specific antigen (PSA) in serum samples. A detection limit of 0.8 ng/mL was achieved for total PSA using the RCM and is at clinically significant concentrations. Comparison of data obtained in a pilot study from the analysis of serum samples with commercially available immunoassays shows good agreement. The development of a quantitative magneto-immunoassay in lateral flow format for total PSA suggests the potential of the RCM to operate with many immunoassay formats. The RCM has the potential to be modified to quantify multiple analytes in this format. This research shows promise for the development of an inexpensive device capable of quantifying multiple analytes at the point-of-care using a magneto-immunoassay in lateral flow format. Full article
(This article belongs to the Special Issue Magnetic Biosensors)
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Figure 1
<p>(<b>a</b>) Diagram of the five coil surface mount sensor and its location and assembly in the Resonant Coil Magnetometer (RCM); (<b>b</b>) Diagram of the Phase Locked Loop (FLL) circuit used with the RCM with the inductive sensor comprised of an array of five flat spiral coils.</p>
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<p>Lateral flow Magneto-immunoassay for Total or Free Prostate Specific Antigen (PSA).</p>
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<p>Relationship of number of Seradyn 760 nm paramagnetic particles (PMPs) and response in the RCM Slope = 2.044 × 10<sup>−7</sup> mV/PMP.</p>
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<p>Photograph of the total PSA lateral flow assay.</p>
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<p>Dose response for total PSA expressed as the average ratio of test to control line by scanning densitometer (SD) (peak height measurements at 380 nm) and by RCM (change in voltage mV) n =3.</p>
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1471 KiB  
Article
Magnetic Properties of FeNi-Based Thin Film Materials with Different Additives
by Cai Liang, Chinthaka P. Gooneratne, Qing Xiao Wang, Yang Liu, Yogesh Gianchandani and Jurgen Kosel
Biosensors 2014, 4(3), 189-203; https://doi.org/10.3390/bios4030189 - 4 Jul 2014
Cited by 17 | Viewed by 7968
Abstract
This paper presents a study of FeNi-based thin film materials deposited with Mo, Al and B using a co-sputtering process. The existence of soft magnetic properties in combination with strong magneto-mechanical coupling makes these materials attractive for sensor applications. Our findings show that [...] Read more.
This paper presents a study of FeNi-based thin film materials deposited with Mo, Al and B using a co-sputtering process. The existence of soft magnetic properties in combination with strong magneto-mechanical coupling makes these materials attractive for sensor applications. Our findings show that FeNi deposited with Mo or Al yields magnetically soft materials and that depositing with B further increases the softness. The out-of-plane magnetic anisotropy of FeNi thin films is reduced by depositing with Al and completely removed by depositing with B. The effect of depositing with Mo is dependent on the Mo concentration. The coercivity of FeNiMo and FeNiAl is reduced to less than a half of that of FeNi, and a value as low as 40 A/m is obtained for FeNiB. The surfaces of the obtained FeNiMo, FeNiAl and FeNiB thin films reveal very different morphologies. The surface of FeNiMo shows nano-cracks, while the FeNiAl films show large clusters and fewer nano-cracks. When FeNi is deposited with B, a very smooth morphology is obtained. The crystal structure of FeNiMo strongly depends on the depositant concentration and changes into an amorphous structure at a higher Mo level. FeNiAl thin films remain polycrystalline, even at a very high concentration of Al, and FeNiB films are amorphous, even at a very low concentration of B. Full article
(This article belongs to the Special Issue Magnetic Biosensors)
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Graphical abstract

Graphical abstract
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<p>SEM images of the surface morphology evolutions of FeNiAl, FeNiMo and FeNiB with various Al, Mo and B contents.</p>
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<p>XRD spectrum of thin films, Al, Mo, FeNi, FeNiAl, FeNiMo and FeNiB. Mo exhibited a body-centered cubic (BCC) polycrystalline structure. Al and FeNi exhibited a face-centered cubic (FCC) polycrystalline.</p>
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<p>HRTEM images with selected area of diffraction (SAD) insets. (<b>a</b>) FeNiB thin film with 9.2 at% B, (<b>b</b>) FeNiAl thin film with 26.9 at% Al and (<b>c</b>) FeNiMo thin film with 11.3 at% Mo.</p>
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<p>Magnetization loops for (<b>a</b>) FeNiAl, (<b>b</b>) FeNiMo and (<b>c</b>) FeNiB, at various concentrations of Al, Mo and B.</p>
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<p>AFM and MFM images of FeNi thin film. (<b>a</b>) AFM images in 2D and 3D; (<b>b</b>) MFM images in 2D and 3D.</p>
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<p>AFM and MFM images (size: 3 µm × 3 µm) of FeNiAl thin films in 3D visualization.</p>
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<p>AFM and MFM images (size: 3 µm × 3 µm) of FeNiMo thin films in 3D visualization.</p>
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<p>AFM and MFM images (size: 3 µm × 3 µm) of FeNiB thin films.</p>
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