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Advances in Luciferase

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 30 August 2024 | Viewed by 591

Special Issue Editor


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Guest Editor
Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Japan
Interests: bioluminescence; luciferase

Special Issue Information

Dear Colleagues,

Bioluminescence, the production of light without heat by living organisms, has elicited the interest of scientists for a long time. The biological functions of bioluminescence are thought to involve defense against predators, assistance in predation, communication in reproduction, and metabolic as well as biochemical pathway byproduct formation in organisms. On the other hand, bioluminescence is the emission of light based on the luciferin–luciferase enzymatic reaction in living organisms. Light signals from bioluminescence reactions are available for bioanalysis and bioreporters for gene expression, in vitro, in vivo, and ex vivo bioimaging, immunoassays, and other applications. Additionally, based on the biosynthesis of luciferin, beetle bioluminescence can detect pesticides, or fungus luminescence can produce auto-luminescence in plants; therefore, the possibilities of bioluminescence system could be infinite. This open access Special Issue will bring together original research and review articles on basic applications of bioluminescence systems and on new knowledge of luciferase as well as luciferin. It highlights new discoveries, approaches, and technical developments in bioluminescence research. The main feature of this Special Issue is to provide open source sharing of significant work.

Topics of this Special Issue include, but are not limited to, the following:

  • Applications of bioluminescence systems, including gene expression analysis, in vitro, in vivo, and ex vivo bioimaging, immunoassays, etc.;
  • Cloning and characterization of new luciferase;
  • Determining the biosynthesis pathway of luciferin;
  • Identifying new luciferin from bioluminescence organisms;
  • Modification and characterization of luciferase or luciferin;
  • Molecular mechanisms of luciferin–luciferase reactions.

Dr. Yoshhiro Ohmiya
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • bioluminescence
  • bioimaging
  • biosynthesis
  • color modulation evolution
  • immunoassay
  • immunohistrochemistry
  • light signal
  • luciferase
  • luciferin
  • luciferase modification
  • luciferin biosynthesis
  • luciferin modification
  • molecular mechnism
  • screening
  • structure
  • toxycological test

Published Papers (1 paper)

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Research

15 pages, 3451 KiB  
Article
Multiplex Detection of Fluorescent Chemokine Binding to CXC Chemokine Receptors by NanoBRET
by Justyna M. Adamska, Spyridon Leftheriotis, Reggie Bosma, Henry F. Vischer and Rob Leurs
Int. J. Mol. Sci. 2024, 25(9), 5018; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms25095018 - 04 May 2024
Viewed by 271
Abstract
NanoLuc-mediated bioluminescence resonance energy transfer (NanoBRET) has gained popularity for its ability to homogenously measure ligand binding to G protein-coupled receptors (GPCRs), including the subfamily of chemokine receptors. These receptors, such as ACKR3, CXCR4, CXCR3, play a crucial role in the regulation of [...] Read more.
NanoLuc-mediated bioluminescence resonance energy transfer (NanoBRET) has gained popularity for its ability to homogenously measure ligand binding to G protein-coupled receptors (GPCRs), including the subfamily of chemokine receptors. These receptors, such as ACKR3, CXCR4, CXCR3, play a crucial role in the regulation of the immune system, are associated with inflammatory diseases and cancer, and are seen as promising drug targets. The aim of this study was to optimize NanoBRET-based ligand binding to NLuc-ACKR3 and NLuc-CXCR4 using different fluorescently labeled chemokine CXCL12 analogs and their use in a multiplex NanoBRET binding assay of two chemokine receptors at the same time. The four fluorescent CXCL12 analogs (CXCL12-AZD488, -AZD546, -AZD594, -AZD647) showed high-affinity saturable binding to both NLuc-ACKR3 and NLuc-CXCR4, with relatively low levels of non-specific binding. Additionally, the binding of all AZDye-labeled CXCL12s to Nluc receptors was inhibited by pharmacologically relevant unlabeled chemokines and small molecules. The NanoBRET binding assay for CXCL10-AZD488 binding to Nluc-CXCR3 was also successfully established and successfully employed for the simultaneous measurement of the binding of unlabeled small molecules to NLuc-CXCR3 and NLuc-CXCR4. In conclusion, multiplexing the NanoBRET-based competition binding assay is a promising tool for testing unlabeled (small) molecules against multiple GPCRs simultaneously. Full article
(This article belongs to the Special Issue Advances in Luciferase)
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