Special Issue "Thioredoxin and Glutathione Systems"
Deadline for manuscript submissions: closed (15 March 2015)
Dr. Angela Calderon
Department of Drug Discovery and Development, Harrison School of Pharmacy, Auburn University, 4306B Walker Building, Auburn, AL 36849, USA
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Interests: biomedical applications of mass spectrometry; natural products drug discovery for infectious diseases; development of LC-MS based bioassays and analytical methods; LC-MS based metabolomic studies; identification and quantitative analysis of proteins and peptides using LC-MS; qNMR based quantitative analysis; In vitro assessment of stability, metabolism and bioavailability of natural products.
Thioredoxin and glutathione systems are part of the antioxidant systems present in various organisms, varying from Archea to man. Proteins on the cell surface, or in the extracellular environment, are rich in stabilizing disulfides, reflecting oxidizing conditions. In contrast, the intracellular environment is kept reduced and proteins contain many free sulfhydryl groups; disulfides are rare. The major ubiquitous disulfide reductase, responsible for maintaining proteins in their reduced state, is thioredoxin, which is reduced by electrons from NADPH via thioredoxin reductase. The other major factor generally responsible for the low redox potential and high free SH content within the cells, is glutathione (GSH), present in millimolar concentrations and kept reduced by NADPH and glutathione reductase. GSH-dependent disulfide reductions are catalyzed by glutaredoxins overlapping the functions of thioredoxins, but are uniquely reactive with GSH-mixed disulfides. Thiol ± disulfide exchange reactions via redox active disulfides, are efficient for electron transport, and are involved in the mechanisms of essential enzymes, such as ribonucleotide reductase, which is required to provide deoxyribonucleotides for DNA synthesis. Thiol ± disulfide exchange reactions, which are rapid and readily reversible, are also ideally suited to control protein function via the redox state of structural or catalytic SH groups. Oxidation of a critical SH group will generally lead to a changed biological function.
The present special issue focuses on thioredoxin and glutathione systems as targets for drug discovery. All aspects related to drug discovery based on the thioredoxin and glutathione systems will be covered in this Special Issue. It is, therefore, a pleasure to invite high quality studies, as well as timely review papers, on target validation, development of new screening assays to find enzyme inhibitors of thioredoxin and glutathione systems, screening for inhibitors from natural products and synthetic compounds libraries, lead optimization of inhibitors, design of selective inhibitors, investigations on the pharmacodynamics and pharmacokinetics, as well as structure–activity relationships of natural products and synthetic inhibitors of thioredoxin and glutathione systems and future research perspectives.
Dr. Angela I. Calderón
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 1800 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.
- natural products
- synthetic compounds
- infectious diseases
- diseases related to oxidative stress
- target validation
- screening assays
- structure–activity relationship
- drug design to improve inhibitor selectivity
- lead optimization
- future research perspectives in the systems