Advances in Redox Biosensor

A special issue of Antioxidants (ISSN 2076-3921).

Deadline for manuscript submissions: closed (30 October 2024) | Viewed by 1689

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Guest Editor
College of Life Sciences and Biotechnology, Korea University, Seoul 02841, Republic of Korea
Interests: methionine oxidation; methionine restriction; aging; methionine sulfoxide reductase; redox biosensors
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Special Issue Information

Dear Colleagues,

Oxidative stress is associated with the onset of various diseases through damage accumulation and often regulates signal transduction and protein function in living organisms. It introduces the utilization of redox enzymes and low-molecular-weight substances as a defense mechanism against oxidative stress and their involvement in regulating intracellular signaling and protein function through changes in redox status. Additionally, it emphasizes efforts to precisely measure and analyze changes in redox status at the molecular level to comprehend metabolic regulatory mechanisms and the etiology and progression of diseases. In particular, the recent use of redox biosensors to detect various diseases highlights active efforts to understand metabolic regulation processes.

We invite you to submit your latest research findings or review articles to this Special Issue, entitled “Advances in Redox Biosensors”, which will bring together current research concerning advances in redox biosensors. We welcome submissions concerning the manipulation of redox biosensors based on DNA, RNA, protein, and nanomaterials and a variety of applications, including detection of redox status changes, diagnosis of disease progression, analysis of metabolic changes and protein function, etc. We believe that this Special Issue will help to highlight the most recent advances in all aspects of redox biosensors and their various applications.

We look forward to receiving your contributions.

Dr. Byung Cheon Lee
Guest Editor

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Keywords

  • redox biosensors
  • various applications of redox biosensors
  • sensing of redox status
  • diagnosis
  • metabolic analysis

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Published Papers (1 paper)

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Research

15 pages, 5035 KiB  
Article
Development and Optimization of a Redox Enzyme-Based Fluorescence Biosensor for the Identification of MsrB1 Inhibitors
by Hyun Bo Shim, Hyunjeong Lee, Hwa Yeon Cho, Young Ho Jo, Lionel Tarrago, Hyunggee Kim, Vadim N. Gladyshev and Byung Cheon Lee
Antioxidants 2024, 13(11), 1348; https://doi.org/10.3390/antiox13111348 - 2 Nov 2024
Viewed by 1258
Abstract
MsrB1 is a thiol-dependent enzyme that reduces protein methionine-R-sulfoxide and regulates inflammatory response in macrophages. Therefore, MsrB1 could be a promising therapeutic target for the control of inflammation. To identify MsrB1 inhibitors, we construct a redox protein-based fluorescence biosensor composed of [...] Read more.
MsrB1 is a thiol-dependent enzyme that reduces protein methionine-R-sulfoxide and regulates inflammatory response in macrophages. Therefore, MsrB1 could be a promising therapeutic target for the control of inflammation. To identify MsrB1 inhibitors, we construct a redox protein-based fluorescence biosensor composed of MsrB1, a circularly permutated fluorescent protein, and the thioredoxin1 in a single polypeptide chain. This protein-based biosensor, named RIYsense, efficiently measures protein methionine sulfoxide reduction by ratiometric fluorescence increase. We used it for high-throughput screening of potential MsrB1 inhibitors among 6868 compounds. A total of 192 compounds were selected based on their ability to reduce relative fluorescence intensity by more than 50% compared to the control. Then, we used molecular docking simulations of the compound on MsrB1, affinity assays, and MsrB1 activity measurement to identify compounds with reliable and strong inhibitory effects. Two compounds were selected as MsrB1 inhibitors: 4-[5-(4-ethylphenyl)-3-(4-hydroxyphenyl)-3,4-dihydropyrazol-2-yl]benzenesulfonamide and 6-chloro-10-(4-ethylphenyl)pyrimido[4,5-b]quinoline-2,4-dione. They are heterocyclic, polyaromatic compounds with a substituted phenyl moiety interacting with the MsrB1 active site, as revealed by docking simulation. These compounds were found to decrease the expression of anti-inflammatory cytokines such as IL-10 and IL-1rn, leading to auricular skin swelling and increased thickness in an ear edema model, effectively mimicking the effects observed in MsrB1 knockout mice. In summary, using a novel redox protein-based fluorescence biosensor, we identified potential MsrB1 inhibitors that can regulate the inflammatory response, particularly by influencing the expression of anti-inflammatory cytokines. These compounds are promising tools for understanding MsrB1’s role during inflammation and eventually controlling inflammation in therapeutic approaches. Full article
(This article belongs to the Special Issue Advances in Redox Biosensor)
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