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Fluorescent Protein Sensors

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

Deadline for manuscript submissions: closed (31 July 2023) | Viewed by 2613

Special Issue Editors


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Guest Editor
State Key Laboratory of Precesion Spectroscopy, East China Normal University, Shanghai, China
Interests: fluorescent sensors; metal nanoclusters; fluoresent proteins; time-resolved fluorescence spectroscopy
Associate professor, School of Science, Jiangnan University, Wuxi, China
Interests: fluorescent protein; time-resolved fluorescence; FLIM; luminous mechanism

Special Issue Information

Dear Colleagues,

In the past few decades, fluorescent proteins have been one of the most important tools in the field of life science. This is mainly due to their outstanding luminescence, excellent biological compatibility, and accurate positioning by genetic encoding. Currently, fluorescent proteins are widely applied in cell imaging, labeling interactions between proteins, constructing biological sensors, and so on. Since the discovery of GFP from the jellyfish Aequorea victoria, fluorescent proteins have been improved significantly. By mutating amino acids, nowadays, there are more choices in excitation and emission wavelengths. The photostability and photobleaching also can be controlled according to the specific use scenario. Additionally, to support improvement, the luminescence mechanism of fluorescent proteins has attracted more and more attention. In recent years, some new classes of fluorescent proteins, such as DsRed from the coral Discosoma, have also been discovered, which further expands its potential applications.

This Special Issue encourages authors to submit new research results concerning mechanism analysis, structure designs, and application innovations for fluorescent protein sensors.

The Special Issue topics include but are not limited to:

New sensor design;

Novel applications;

Cell visualization;

Subcelluar localization;

Protein–protein interactions;

The luminous mechanism;

Structure analysis; and

Ultrafast spectroscopy analysis.

Dr. Sanjun Zhang
Dr. Lei Li
Guest Editors

Manuscript Submission Information

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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.

Published Papers (1 paper)

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Research

15 pages, 2186 KiB  
Article
Development of a Real-Time Pectic Oligosaccharide-Detecting Biosensor Using the Rapid and Flexible Computational Identification of Non-Disruptive Conjugation Sites (CINC) Biosensor Design Platform
by Dustin D. Smith, Joshua P. King, D. Wade Abbott and Hans-Joachim Wieden
Sensors 2022, 22(3), 948; https://doi.org/10.3390/s22030948 - 26 Jan 2022
Viewed by 2106
Abstract
Fluorescently labeled, solute-binding proteins that change their fluorescent output in response to ligand binding are frequently used as biosensors for a wide range of applications. We have previously developed a “Computational Identification of Non-disruptive Conjugation sites” (CINC) approach, an in silico pipeline utilizing [...] Read more.
Fluorescently labeled, solute-binding proteins that change their fluorescent output in response to ligand binding are frequently used as biosensors for a wide range of applications. We have previously developed a “Computational Identification of Non-disruptive Conjugation sites” (CINC) approach, an in silico pipeline utilizing molecular dynamics simulations for the rapid design and construction of novel protein–fluorophore conjugate-type biosensors. Here, we report an improved in silico scoring algorithm for use in CINC and its use in the construction of an oligogalacturonide-detecting biosensor set. Using both 4,5-unsaturated and saturated oligogalacturonides, we demonstrate that signal transmission from the ligand-binding pocket of the starting protein scaffold to the CINC-selected reporter positions is effective for multiple different ligands. The utility of an oligogalacturonide-detecting biosensor is shown in Carbohydrate Active Enzyme (CAZyme) activity assays, where the biosensor is used to follow product release upon polygalacturonic acid (PGA) depolymerization in real time. The oligogalacturonide-detecting biosensor set represents a novel enabling tool integral to our rapidly expanding platform for biosensor-based carbohydrate detection, and moving forward, the CINC pipeline will continue to enable the rational design of biomolecular tools to detect additional chemically distinct oligosaccharides and other solutes. Full article
(This article belongs to the Special Issue Fluorescent Protein Sensors)
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