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Sensors for Glycoproteins and Glycated Proteins

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Special Issue Information
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Published Papers

A special issue of Sensors (ISSN 1424-8220). This special issue belongs to the section "Biosensors".

Deadline for manuscript submissions: closed (15 May 2017) | Viewed by 47365

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Special Issue Editor

Prof. Dr. Junichi Anzai

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Guest Editor

Graduate School of Pharmaceutical Sciences Tohoku University Aoba 6-3, Aramaki, Aoba-ku, Sendai 980-8578, Japan
Interests: biosensors; layer-by-layer films; microcapsules

Special Issue Information

Dear Colleagues,

This Special Issue focuses on biosensors for glycoproteins and glycated proteins. Biosensors for any type of glycoproteins, extrinsically glycated proteins, such as HbA1c and related compounds, are considered for publication in this Special Issue. These biosensors include optical sensors, such as colorimetric and fluorometric sensors, as well as electrochemical sensors in amperometric, voltametric, impedimetric, and potentiometric detection modes. Other biosensors, such as quartz crystal microbalance (QCM) sensors, are also welcome. Biosensors applicable to biomedical analysis, environmental monitoring, process control in food and pharmaceutical industries, and biological research are within the scope of this Special Issue. Submission of papers dealing with the construction of high-performance of biosensors based on metal and carbon nanomaterials is particularly encouraged. Both original research papers and review articles on the basic principle and applications of biosensors are solicited.

This Special Issue aims to promote the exchanges of ideas and the knowledge of scientists and engineers working in the communities of biosensors.

Prof. Dr. Junichi Anzai
Guest Editor

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 submissions that pass pre-check are 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. Sensors is an international peer-reviewed open access semimonthly 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 2600 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

Optical and electrochemical sensors
Colorimetric and fluorometric sensors
Quartz crystal microbalance sensors
Enzyme sensors
Immunosensors
Aptamer sensors
Glycoproteins and glycated proteins
Lectin-based sensors
Glycated haemoglobin (HbA1c) sensors

Published Papers (6 papers)

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Research

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531 KiB

Open AccessArticle

Exploitation of SPR to Investigate the Importance of Glycan Chains in the Interaction between Lactoferrin and Bacteria

by Noelle O’Riordan, Michelle Kilcoyne, Lokesh Joshi and Rita M. Hickey

Sensors 2017, 17(7), 1515; https://doi.org/10.3390/s17071515 - 27 Jun 2017

Cited by 2 | Viewed by 4060

Abstract

Bovine lactoferrin (LF) has been shown to prevent adhesion to and invasion of mammalian cell lines by pathogenic bacteria, with evidence for direct bacterial binding by the milk glycoprotein. However, the glycosylation pattern of LF changes over the lactation cycle. In this study, we aim to investigate the effect that this variation has on the milk glycoprotein’s ability to interact with pathogens. Surface plasmon resonance technology was employed to compare the binding of LF from colostrum (early lactation) and mature milk (late lactation) to a panel of pathogenic bacteria (Staphylococcus aureus, Escherichia coli, Cronobacter sakazakii, Streptococcus pneumoniae, Pseudomonas aeruginosa, Listeria monocytogenes and Salmonella typhimurium). Novel interactions with LF were identified for C. sakazakii, S. pneumoniae and P. aeruginosa with the highest binding ability observed for mature milk LF in all cases, with the exception of S. typhimurium. The difference in bacterial binding observed may be as a result of the varying glycosylation profiles. This work demonstrates the potential of LF as a functional food ingredient to prevent bacterial infection. Full article

(This article belongs to the Special Issue Sensors for Glycoproteins and Glycated Proteins)

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3225 KiB

Open AccessArticle

RAGE Plays a Role in LPS-Induced NF-κB Activation and Endothelial Hyperpermeability

by Liqun Wang, Jie Wu, Xiaohua Guo, Xuliang Huang and Qiaobing Huang

Sensors 2017, 17(4), 722; https://doi.org/10.3390/s17040722 - 30 Mar 2017

Cited by 45 | Viewed by 7173

Abstract

Endothelial functional dysregulation and barrier disruption contribute to the initiation and development of sepsis. The receptor for advanced glycation end products (RAGE) has been demonstrated to be involved in the pathogenesis of sepsis. The present study aimed to investigate the role of RAGE in lipopolysaccharide (LPS)-induced nuclear factor-κB (NF-κB) activation in endothelial cells and the consequent endothelial hyperpermeability. LPS-induced upregulation of RAGE protein expression in human umbilical vein endothelial cells (HUVECs) was detected by western blotting. Activation of NF-κB was revealed using western blotting and immunofluorescent staining. LPS-elicited endothelial hyperpermeability was explored by transendothelial electrical resistance (TER) assay and endothelial monolayer permeability assay. The blocking antibody specific to RAGE was used to confirm the role of RAGE in LPS-mediated NF-κB activation and endothelial barrier disruption. We found that LPS upregulated the protein expression of RAGE in a dose- and time-dependent manner in HUVECs. Moreover, LPS triggered a significant phosphorylation and degradation of IκBα, as well as NF-κB p65 nuclear translocation. Moreover, we observed a significant increase in endothelial permeability after LPS treatment. However, the RAGE blocking antibody attenuated LPS-evoked NF-κB activation and endothelial hyperpermeability. Our results suggest that RAGE plays an important role in LPS-induced NF-κB activation and endothelial barrier dysfunction. Full article

(This article belongs to the Special Issue Sensors for Glycoproteins and Glycated Proteins)

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1481 KiB

Open AccessCommunication

Label-Free Detection of Human Glycoprotein (CgA) Using an Extended-Gated Organic Transistor-Based Immunosensor

by Tsukuru Minamiki, Tsuyoshi Minami, Yui Sasaki, Shin-ichi Wakida, Ryoji Kurita, Osamu Niwa and Shizuo Tokito

Sensors 2016, 16(12), 2033; https://doi.org/10.3390/s16122033 - 30 Nov 2016

Cited by 29 | Viewed by 7169

Abstract

Herein, we report on the fabrication of an extended-gated organic field-effect transistor (OFET)-based immunosensor and its application in the detection of human chromogranin A (hCgA). The fabricated OFET device possesses an extended-gate electrode immobilized with an anti-CgA antibody. The titration results of hCgA showed that the electrical changes in the OFET characteristics corresponded to the glycoprotein recognition ability of the monoclonal antibody (anti-CgA). The observed sensitivity (detection limit: 0.11 µg/mL) and selectivity indicate that the OFET-based immunosensor can be potentially applied to the rapid detection of the glycoprotein concentration without any labeling. Full article

(This article belongs to the Special Issue Sensors for Glycoproteins and Glycated Proteins)

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2914 KiB

Open AccessArticle

Single-Use Disposable Electrochemical Label-Free Immunosensor for Detection of Glycated Hemoglobin (HbA1c) Using Differential Pulse Voltammetry (DPV)

by Alireza Molazemhosseini, Luca Magagnin, Pasquale Vena and Chung-Chiun Liu

Sensors 2016, 16(7), 1024; https://doi.org/10.3390/s16071024 - 01 Jul 2016

Cited by 42 | Viewed by 10268

Abstract

A single-use disposable in vitro electrochemical immunosensor for the detection of HbA1c in undiluted human serum using differential pulse voltammetry (DPV) was developed. A three-electrode configuration electrochemical biosensor consisted of 10-nm-thin gold film working and counter electrodes and a thick-film printed Ag/AgCl reference electrode was fabricated on a polyethylene terephthalate (PET) substrate. Micro-fabrication techniques including sputtering vapor deposition and thick-film printing were used to fabricate the biosensor. This was a roll-to-roll cost-effective manufacturing process making the single-use disposable in vitro HbA1c biosensor a reality. Self-assembled monolayers of 3-Mercaptopropionic acid (MPA) were employed to covalently immobilize anti-HbA1c on the surface of gold electrodes. Electrochemical impedance spectroscopy (EIS) and X-ray photoelectron spectroscopy (XPS) confirmed the excellent coverage of MPA-SAM and the upward orientation of carboxylic groups. The hindering effect of HbA1c on the ferricyanide/ferrocyanide electron transfer reaction was exploited as the HbA1c detection mechanism. The biosensor showed a linear range of 7.5–20 µg/mL of HbA1c in 0.1 M PBS. Using undiluted human serum as the test medium, the biosensor presented an excellent linear behavior (R² = 0.999) in the range of 0.1–0.25 mg/mL of HbA1c. The potential application of this biosensor for in vitro measurement of HbA1c for diabetic management was demonstrated. Full article

(This article belongs to the Special Issue Sensors for Glycoproteins and Glycated Proteins)

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Review

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2705 KiB

Open AccessReview

Current Status of HbA1c Biosensors

by Hua Lin and Jun Yi

Sensors 2017, 17(8), 1798; https://doi.org/10.3390/s17081798 - 04 Aug 2017

Cited by 31 | Viewed by 10361

Abstract

Glycated hemoglobin (HbA1c) is formed via non-enzymatic glycosylation reactions at the α–amino group of βVal1 residues in the tetrameric Hb, and it can reflect the ambient glycemic level over the past two to three months. A variety of HbA1c detection methods, including chromatography, immunoassay, enzymatic measurement, electrochemical sensor and capillary electrophoresis have been developed and used in research laboratories and in clinics as well. In this review, we summarize the current status of HbA1c biosensors based on the recognition of the sugar moiety on the protein and also their applications in the whole blood sample measurements. Full article

(This article belongs to the Special Issue Sensors for Glycoproteins and Glycated Proteins)

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3051 KiB

Open AccessReview

Recent Progress in Electrochemical Biosensors for Glycoproteins

by Uichi Akiba and Jun-ichi Anzai

Sensors 2016, 16(12), 2045; https://doi.org/10.3390/s16122045 - 01 Dec 2016

Cited by 25 | Viewed by 7695

Abstract

This review provides an overview of recent progress in the development of electrochemical biosensors for glycoproteins. Electrochemical glycoprotein sensors are constructed by combining metal and carbon electrodes with glycoprotein-selective binding elements including antibodies, lectin, phenylboronic acid and molecularly imprinted polymers. A recent trend in the preparation of glycoprotein sensors is the successful use of nanomaterials such as graphene, carbon nanotube, and metal nanoparticles. These nanomaterials are extremely useful for improving the sensitivity of glycoprotein sensors. This review focuses mainly on the protocols for the preparation of glycoprotein sensors and the materials used. Recent improvements in glycoprotein sensors are discussed by grouping the sensors into several categories based on the materials used as recognition elements. Full article

(This article belongs to the Special Issue Sensors for Glycoproteins and Glycated Proteins)

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