Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
7.3
3.4
Journals
Sensors
Special Issues
Protein-Based Biosensors
sensors-logo
Submit to Sensors Review for Sensors Propose a Special Issue

Journal Menu

► Journal Menu

Journal Browser

► Journal Browser
share announcement

Protein-Based Biosensors

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

Deadline for manuscript submissions: closed (31 August 2018) | Viewed by 39730

Special Issue Editors

Prof. Paola Giardina

E-Mail
Guest Editor
Department of Chemical Sciences, Università degli Studi di Napoli Federico II, Naples, Italy
Interests: fungal proteins; proteic biosurfactants; surface modification; hydrophobins; functional amyloids
Special Issues, Collections and Topics in MDPI journals
Dr. Alessandra Piscitelli

E-Mail Website
Guest Editor
Department of Chemical Sciences, University of Naples “Federico II”, Via Cintia 4, I-80126 Naples, Italy
Interests: protein recombinant expression; biosensing; protein immobilization, fungal laccase
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

A key step of the development of biosensors is the biological interfacing of materials. The design and the realization of bio/non-bio interfaces with specific properties and performances are crucial features in bio-device development. Indeed, the development of sensitive and reproducible biosensor surfaces needs the immobilization of active proteins with a controllable and homogeneous orientation to complementary functionalized surfaces. This achievement is however extremely dependent on the protein of interest.

We would like to invite you to submit a manuscript to the Special Issue we are Guest-Editing, entitled “Proteins Based Biosensors”, to be published in the beginning of 2018. The aim of this Special Issue is to collect research or review papers dedicated to the exploitation of proteins in the field of biosensing. Special emphasis will be devoted to novel approaches to protein immobilization on conventional surfaces, nanoparticles, or 2D materials.

Prof. Dr. Paola Giardina
Dr. Alessandra Piscitelli
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 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

  • enzyme immobilization
  • hybrid interfaces
  • self-assembled layers
  • protein layers
  • nanoparticles
  • 2D materials

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • e-Book format: Special Issues with more than 10 articles can be published as dedicated e-books, ensuring wide and rapid dissemination.

Further information on MDPI's Special Issue polices can be found here.

Published Papers (6 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

Jump to: Review

15 pages, 9674 KiB  
Article
Experimental Study of the Oriented Immobilization of Antibodies on Photonic Sensing Structures by Using Protein A as an Intermediate Layer
by Raffaele Caroselli, Javier García Castelló, Jorge Escorihuela, María José Bañuls, Ángel Maquieira and Jaime García-Rupérez
Sensors 2018, 18(4), 1012; https://doi.org/10.3390/s18041012 - 28 Mar 2018
Cited by 14 | Viewed by 4847
Abstract
A proper antibody immobilization on a biosensor is a crucial step in order to obtain a high sensitivity to be able to detect low target analyte concentrations. In this paper, we present an experimental study of the immobilization process of antibodies as bioreceptors [...] Read more.
A proper antibody immobilization on a biosensor is a crucial step in order to obtain a high sensitivity to be able to detect low target analyte concentrations. In this paper, we present an experimental study of the immobilization process of antibodies as bioreceptors on a photonic ring resonator sensor. A protein A intermediate layer was created on the sensor surface in order to obtain an oriented immobilization of the antibodies, which enhances the interaction with the target antigens to be detected. The anti-bovine serum albumin (antiBSA)-bovine serum albumin (BSA) pair was used as a model for our study. An opto-fluidic setup was developed in order to flow the different reagents and, simultaneously, to monitor in real-time the spectral response of the photonic sensing structure. The antiBSA immobilization and the BSA detection, their repeatability, and specificity were studied in different conditions of the sensor surface. Finally, an experimental limit of detection for BSA recognition of only 1 ng/mL was obtained. Full article
(This article belongs to the Special Issue Protein-Based Biosensors)
►▼ Show Figures

Figure 1

10 pages, 1293 KiB  
Article
Detection of Matrix Metalloproteinase Activity by Bioluminescence via Intein-Mediated Biotinylation of Luciferase
by Duc Long Nguyen, Hanim Kim, Dasom Kim, Jin Oh Lee, Myung Chan Gye and Young-Pil Kim
Sensors 2018, 18(3), 875; https://doi.org/10.3390/s18030875 - 15 Mar 2018
Cited by 9 | Viewed by 5740
Abstract
We report bioluminescence analysis of matrix metalloproteinase (MMP) activity in biological substances using a surface-bound luciferase probe. Intein-fused luciferase protein enables site-specific biotinylation of luciferase in the presence of N-terminus cysteine-biotin via intein-mediated splicing process, resulting in a strong association with high bioluminescence [...] Read more.
We report bioluminescence analysis of matrix metalloproteinase (MMP) activity in biological substances using a surface-bound luciferase probe. Intein-fused luciferase protein enables site-specific biotinylation of luciferase in the presence of N-terminus cysteine-biotin via intein-mediated splicing process, resulting in a strong association with high bioluminescence signal onto a NeutrAvidin-coated surface. When the peptide substrate for MMP-7 was inserted into a region between luciferase and intein, the biotinylated probe detected MMP-7 activity by cleaving the peptide, and surface-induced bioluminescence signal was strongly reduced in the MMP-secreted media or mouse tissue extracts, compared with that in MMP-deficient control set. Our approach is anticipated to be useful for generating biotinylated proteins and for their applications in diagnosing MMP activity in human diseases. Full article
(This article belongs to the Special Issue Protein-Based Biosensors)
►▼ Show Figures

Figure 1

11 pages, 1500 KiB  
Article
A New Method for Immobilization of His-Tagged Proteins with the Application of Low-Frequency AC Electric Field
by Shunsuke Takahashi, Kazuki Kishi, Ryota Hiraga, Kazuki Hayashi, Youhei Mamada, Masahiko Oshige and Shinji Katsura
Sensors 2018, 18(3), 784; https://doi.org/10.3390/s18030784 - 5 Mar 2018
Cited by 6 | Viewed by 5478
Abstract
Continued advancement of protein array, bioelectrode, and biosensor technologies is necessary to develop methods for higher amount and highly oriented immobilization activity of proteins. In pursuit of these goals, we developed a new immobilization method by combining electrostatic transport and subsequent molecular diffusion [...] Read more.
Continued advancement of protein array, bioelectrode, and biosensor technologies is necessary to develop methods for higher amount and highly oriented immobilization activity of proteins. In pursuit of these goals, we developed a new immobilization method by combining electrostatic transport and subsequent molecular diffusion of protein molecules. Our developed immobilization method is based on a model that transports proteins toward the substrate surface due to steep concentration gradient generated by low-frequency AC electric field. The immobilization of the maximum amounts can be obtained by the application of the AC voltage of 80 Vpp, 20 Hz both for His-tagged Green Fluorescent Protein (GFP) and Discosoma sp. Red Fluorescent Protein (DsRed), used as model proteins. The amounts of the immobilized His-tagged GFP and DsRed were approximately seven-fold higher than that in the absence of the application of low-frequency AC electric field. Furthermore, the positively and negatively charged His-tagged GFP at acidic and alkaline pH were immobilized by applying of low-frequency AC electric field, whereas the non-charged His-tagged GFP at the pH corresponding to its isoelectric point (pI) was not immobilized. Therefore, unless the pH is equal to pI, the immobilization of electrically charged proteins was strongly enhanced through electrostatic transport and subsequent molecular diffusion. Full article
(This article belongs to the Special Issue Protein-Based Biosensors)
►▼ Show Figures

Figure 1

1971 KiB  
Article
Ultra-Sensitive NT-proBNP Quantification for Early Detection of Risk Factors Leading to Heart Failure
by Keum-Soo Song, Satish Balasaheb Nimse, Mukesh Digambar Sonawane, Shrikant Dashrath Warkad and Taisun Kim
Sensors 2017, 17(9), 2116; https://doi.org/10.3390/s17092116 - 14 Sep 2017
Cited by 20 | Viewed by 6867
Abstract
Cardiovascular diseases such as acute myocardial infarction and heart failure accounted for the death of 17.5 million people (31% of all global deaths) in 2015. Monitoring the level of circulating N-terminal proBNP (NT-proBNP) is crucial for the detection of people at risk of [...] Read more.
Cardiovascular diseases such as acute myocardial infarction and heart failure accounted for the death of 17.5 million people (31% of all global deaths) in 2015. Monitoring the level of circulating N-terminal proBNP (NT-proBNP) is crucial for the detection of people at risk of heart failure. In this article, we describe a novel ultra-sensitive NT-proBNP test (us-NT-proBNP) that allows the quantification of circulating NT-proBNP in 30 min at 25 °C in the linear detection range of 7.0–600 pg/mL. It is a first report on the application of a fluorescence bead labeled detection antibody, DNA-guided detection method, and glass fiber membrane platform for the quantification of NT-proBNP in clinical samples. Limit of blank, limit of detection, and limit of quantification were 2.0 pg/mL, 3.7 pg/mL, and 7 pg/mL, respectively. The coefficient of variation was found to be less than 10% in the entire detection range of 7–600 pg/mL. The test demonstrated specificity for NT-proBNP without interferences from bilirubin, intra-lipid, biotin, and hemoglobin. The serial dilution test for plasma samples containing various NT-proBNP levels showed the linear decrement in concentration with the regression coefficient of 0.980–0.998. These results indicate that us-NT-proBNP test does not suffer from the interference of the plasma components for the measurement of NT-proBNP in clinical samples. Full article
(This article belongs to the Special Issue Protein-Based Biosensors)
►▼ Show Figures

Figure 1

Review

Jump to: Research

19 pages, 1428 KiB  
Review
Odorant-Binding Proteins as Sensing Elements for Odour Monitoring
by Paolo Pelosi, Jiao Zhu and Wolfgang Knoll
Sensors 2018, 18(10), 3248; https://doi.org/10.3390/s18103248 - 27 Sep 2018
Cited by 71 | Viewed by 7932
Abstract
Odour perception has been the object of fast growing research interest in the last three decades. Parallel to the study of the corresponding biological systems, attempts are being made to model the olfactory system with electronic devices. Such projects range from the fabrication [...] Read more.
Odour perception has been the object of fast growing research interest in the last three decades. Parallel to the study of the corresponding biological systems, attempts are being made to model the olfactory system with electronic devices. Such projects range from the fabrication of individual sensors, tuned to specific chemicals of interest, to the design of multipurpose smell detectors using arrays of sensors assembled in a sort of artificial nose. Recently, proteins have attracted increasing interest as sensing elements. In particular, soluble olfaction proteins, including odorant-binding proteins (OBPs) of vertebrates and insects, chemosensory proteins (CSPs) and Niemann-Pick type C2 (NPC2) proteins possess interesting characteristics for their use in sensing devices for odours. In fact, thanks to their compact structure, their soluble nature and small size, they are extremely stable to high temperature, refractory to proteolysis and resistant to organic solvents. Moreover, thanks to the availability of many structures solved both as apo-proteins and in complexes with some ligands, it is feasible to design mutants by replacing residues in the binding sites with the aim of synthesising proteins with better selectivity and improved physical properties, as demonstrated in a number of cases. Full article
(This article belongs to the Special Issue Protein-Based Biosensors)
►▼ Show Figures

Figure 1

1536 KiB  
Review
Achievements and Prospects in Electrochemical-Based Biosensing Platforms for Aflatoxin M1 Detection in Milk and Dairy Products
by Ana-Maria Gurban, Petru Epure, Florin Oancea and Mihaela Doni
Sensors 2017, 17(12), 2951; https://doi.org/10.3390/s17122951 - 19 Dec 2017
Cited by 27 | Viewed by 7798
Abstract
Aflatoxins, which are mainly produced by Aspergillus flavus and parasiticus growing on plants and products stored under inappropriate conditions, represent the most studied group of mycotoxins. Contamination of human and animal milk with aflatoxin M1, the hydroxylated metabolite of aflatoxin B [...] Read more.
Aflatoxins, which are mainly produced by Aspergillus flavus and parasiticus growing on plants and products stored under inappropriate conditions, represent the most studied group of mycotoxins. Contamination of human and animal milk with aflatoxin M1, the hydroxylated metabolite of aflatoxin B1, is an important health risk factor due to its carcinogenicity and mutagenicity. Due to the low concentration of this aflatoxin in milk and milk products, the analytical methods used for its quantification have to be highly sensitive, specific and simple. This paper presents an overview of the analytical methods, especially of the electrochemical immunosensors and aptasensors, used for determination of aflatoxin M1. Full article
(This article belongs to the Special Issue Protein-Based Biosensors)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-6
Back to TopTop