[ad_1]
Wang, C. et al. A novel coronavirus outbreak of global health concern. Lancet 395(10223), 470–473 (2020).
Wu, F. et al. A new coronavirus associated with human respiratory disease in China. Nature 579(7798), 265–269 (2020).
Andersen, K. G. et al. The proximal origin of SARS-CoV-2. Nat. Med. 26(4), 450–452 (2020).
Dong, E., Du, H. & Gardner, L. An interactive web-based dashboard to track COVID-19 in real time. Lancet Infect. Dis. 20(5), 533–534 (2020).
Harvey, W. T. et al. SARS-CoV-2 variants, spike mutations and immune escape. Nat. Rev. Microbiol. 19(7), 409–424 (2021).
Heinz, F. X. & Stiasny, K. Distinguishing features of current COVID-19 vaccines: Knowns and unknowns of antigen presentation and modes of action. NPJ Vaccines 6(1), 104 (2021).
Zumla, A. et al. Coronaviruses—Drug discovery and therapeutic options. Nat. Rev. Drug Discov. 15(5), 327–347 (2016).
Elfiky, A. A. Ribavirin, remdesivir, sofosbuvir, galidesivir, and tenofovir against SARS-CoV-2 RNA dependent RNA polymerase (RdRp): A molecular docking study. Life Sci. 253, 117592 (2020).
Jin, Z. et al. Structure of M(pro) from SARS-CoV-2 and discovery of its inhibitors. Nature 582(7811), 289–293 (2020).
Kandeel, M. & Al-Nazawi, M. Virtual screening and repurposing of FDA approved drugs against COVID-19 main protease. Life Sci. 251, 117627 (2020).
Khodadadi, E. et al. Study of combining virtual screening and antiviral treatments of the Sars-CoV-2 (Covid-19). Microb. Pathog. 146, 104241 (2020).
Rameshrad, M. et al. A comprehensive review on drug repositioning against coronavirus disease 2019 (COVID19). Naunyn Schmiedebergs Arch. Pharmacol. 393(7), 1137–1152 (2020).
Joshi, S., Joshi, M. & Degani, M. S. Tackling SARS-CoV-2: Proposed targets and repurposed drugs. Future Med. Chem. 12(17), 1579–1601 (2020).
Beigel, J. H. et al. Remdesivir for the treatment of Covid-19—Final report. N. Engl. J. Med. 383(19), 1813–1826 (2020).
WHOST Consortium. Repurposed antiviral drugs for Covid-19—Interim WHO solidarity trial results. N. Engl. J. Med. 384(6), 497–511 (2021).
Fehr, A. R. & Perlman, S. Coronaviruses: An overview of their replication and pathogenesis. Methods Mol. Biol. 1282, 1–23 (2015).
Hilgenfeld, R. From SARS to MERS: Crystallographic studies on coronaviral proteases enable antiviral drug design. FEBS J. 281(18), 4085–4096 (2014).
Zhang, L. et al. Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved alpha-ketoamide inhibitors. Science 368(6489), 409–412 (2020).
Anand, K. et al. Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs. Science 300(5626), 1763–1767 (2003).
Fan, K. et al. Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase. J. Biol. Chem. 279(3), 1637–1642 (2004).
Goyal, B. & Goyal, D. Targeting the dimerization of the main protease of coronaviruses: A potential broad-spectrum therapeutic strategy. ACS Combin. Sci. 22(6), 297–305 (2020).
Rut, W. et al. SARS-CoV-2 M(pro) inhibitors and activity-based probes for patient-sample imaging. Nat. Chem. Biol. 17(2), 222–228 (2021).
Yang, H. et al. Design of wide-spectrum inhibitors targeting coronavirus main proteases. PLoS Biol. 3(10), e324 (2005).
Freitas, B. T. et al. Characterization and noncovalent inhibition of the deubiquitinase and deISGylase activity of SARS-CoV-2 papain-like protease. ACS Infect. Dis. 6(8), 2099–2109 (2020).
Klemm, T. et al. Mechanism and inhibition of the papain-like protease, PLpro, of SARS-CoV-2. EMBO J. 39(18), e106275 (2020).
Rut, W. et al. Activity profiling and crystal structures of inhibitor-bound SARS-CoV-2 papain-like protease: A framework for anti-COVID-19 drug design. Sci. Adv. 6(42), eabd4596 (2020).
Shin, D. et al. Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity. Nature 587(7835), 657–662 (2020).
Lesser, R. & Weiß, R. Über selenhaltige aromatische Verbindungen (VI). Ber. dtsch. Chem. Ges. A/B 57, 1077–1082 (1924).
Mugesh, G., du Mont, W. W. & Sies, H. Chemistry of biologically important synthetic organoselenium compounds. Chem. Rev. 101(7), 2125–2179 (2001).
Antony, S. & Bayse, C. A. Modeling the mechanism of the glutathione peroxidase mimic ebselen. Inorg. Chem. 50(23), 12075–12084 (2011).
Azad, G. K. & Tomar, R. S. Ebselen, a promising antioxidant drug: Mechanisms of action and targets of biological pathways. Mol. Biol. Rep. 41(8), 4865–4879 (2014).
Sarma, B. K. & Mugesh, G. Antioxidant activity of the anti-inflammatory compound ebselen: A reversible cyclization pathway via selenenic and seleninic acid intermediates. Chemistry 14(34), 10603–10614 (2008).
Bhabak, K. P. & Mugesh, G. Functional mimics of glutathione peroxidase: Bioinspired synthetic antioxidants. Acc. Chem. Res. 43(11), 1408–1419 (2010).
Morgenstern, R., Cotgreave, I. A. & Engman, L. Determination of the relative contributions of the diselenide and selenol forms of ebselen in the mechanism of its glutathione peroxidase-like activity. Chem. Biol. Interact. 84(1), 77–84 (1992).
Sands, K. N. & Back, T. G. Key steps and intermediates in the catalytic mechanism for the reduction of peroxides by the antioxidant ebselen. Tetrahedron 74(38), 4959–4967 (2018).
Sies, H. Ebselen, a selenoorganic compound as glutathione peroxidase mimic. Free Radic. Biol. Med. 14(3), 313–323 (1993).
Wedding, J. L. et al. Investigation into the intracellular fates, speciation and mode of action of selenium-containing neuroprotective agents using XAS and XFM. Biochim. Biophys. Acta Gen. Subj. 1862(11), 2393–2404 (2018).
Weglarz-Tomczak, E. et al. Identification of ebselen and its analogues as potent covalent inhibitors of papain-like protease from SARS-CoV-2. Sci. Rep. 11(1), 3640 (2021).
Amporndanai, K. et al. Inhibition mechanism of SARS-CoV-2 main protease by ebselen and its derivatives. Nat. Commun. 12(1), 3061 (2021).
Cao, J., Forrest, J. C. & Zhang, X. A screen of the NIH Clinical Collection small molecule library identifies potential anti-coronavirus drugs. Antivir. Res. 114, 1–10 (2015).
Mangiavacchi, F. et al. Seleno-functionalization of quercetin improves the non-covalent inhibition of M(pro) and its antiviral activity in cells against SARS-CoV-2. Int. J. Mol. Sci. 22(13), 7048 (2021).
Kasprzyk, R. et al. Identification and evaluation of potential SARS-CoV-2 antiviral agents targeting mRNA cap guanine N7-Methyltransferase. Antivir. Res. 193, 105142 (2021).
Chen, Y. et al. Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase. Proc. Natl. Acad. Sci. U.S.A. 106(9), 3484–3489 (2009).
Bouvet, M. et al. In vitro reconstitution of SARS-coronavirus mRNA cap methylation. PLoS Pathog. 6(4), e1000863 (2010).
Dong, H., Zhang, B. & Shi, P. Y. Flavivirus methyltransferase: A novel antiviral target. Antivir. Res. 80(1), 1–10 (2008).
Tong, T. R. Drug targets in severe acute respiratory syndrome (SARS) virus and other coronavirus infections. Infect. Disord. Drug Targets 9(2), 223–245 (2009).
Hartenian, E. et al. The molecular virology of coronaviruses. J. Biol. Chem. 295(37), 12910–12934 (2020).
Malone, B. et al. Structures and functions of coronavirus replication-transcription complexes and their relevance for SARS-CoV-2 drug design. Nat. Rev. Mol. Cell Biol. 23(1), 21–39 (2022).
Sancineto, L. et al. Design and synthesis of DiselenoBisBenzamides (DISeBAs) as nucleocapsid protein 7 (NCp7) inhibitors with anti-HIV activity. J. Med. Chem. 58(24), 9601–9614 (2015).
Thenin-Houssier, S. et al. Ebselen, a small-molecule capsid inhibitor of HIV-1 replication. Antimicrob. Agents Chemother. 60(4), 2195–2208 (2016).
Sartori, G. et al. Antiviral action of diphenyl diselenide on herpes simplex virus 2 infection in female BALB/c mice. J. Cell. Biochem. 117(7), 1638–1648 (2016).
Mukherjee, S. et al. Ebselen inhibits hepatitis C virus NS3 helicase binding to nucleic acid and prevents viral replication. ACS Chem. Biol. 9(10), 2393–2403 (2014).
Simanjuntak, Y. et al. Ebselen alleviates testicular pathology in mice with Zika virus infection and prevents its sexual transmission. PLoS Pathog. 14(2), e1006854 (2018).
Zhao, R. & Holmgren, A. A novel antioxidant mechanism of ebselen involving ebselen diselenide, a substrate of mammalian thioredoxin and thioredoxin reductase. J. Biol. Chem. 277(42), 39456–39462 (2002).
Azeredo, J. B., Schwab, R. S. & Braga, A. L. Synthesis of biologically active selenium-containing molecules from greener perspectives. Curr. Green Chem. 3(1), 51–67 (2016).
Balkrishna, S. J. et al. An ebselen like catalyst with enhanced GPx activity via a selenol intermediate. Org. Biomol. Chem. 12(8), 1215–1219 (2014).
Balkrishna, S. J. et al. Cu-catalyzed efficient synthetic methodology for ebselen and related Se-N heterocycles. Org. Lett. 12(23), 5394–5397 (2010).
Balkrishna, S. J., Bhakuni, B. S. & Kumar, S. Copper catalyzed/mediated synthetic methodology for ebselen and related isoselenazolones. Tetrahedron 67(49), 9565–9575 (2011).
Osajda, M. & Młochowski, J. The reactions of 2-(chloroseleno)benzoyl chloride with nucleophiles. Tetrahedron 58(37), 7531–7537 (2002).
Giurg, M. et al. Reaction of bis[(2-chlorocarbonyl)phenyl] diselenide with phenols, aminophenols, and other amines towards diphenyl diselenides with antimicrobial and antiviral properties. Molecules 22(6), 974 (2017).
Mlochowski, J. et al. Synthesis and properties of 2-carboxyalkyl-1,2-benzisoselenazol-3(2H)-ones and related organoselenium compounds as nitric oxide synthase inhibitors and cytokine inducers. Liebigs Ann. 1996(11), 1751–1755 (1996).
Giurg, M. & Syper, L. Diaryl diselenides and related compounds as oxygen-transfer agents. Phosphorus Sulfur Silicon Relat. Elem. 183(4), 970–985 (2008).
Piętka-Ottlik, M. et al. Synthesis of new alkylated and methoxylated analogues of ebselen with antiviral and antimicrobial properties. ARKIVOC 2017(2), 546–556 (2017).
Weglarz-Tomczak, E. et al. Identification of methionine aminopeptidase 2 as a molecular target of the organoselenium drug ebselen and its derivatives/analogues: Synthesis, inhibitory activity and molecular modeling study. Bioorg. Med. Chem. Lett. 26(21), 5254–5259 (2016).
Bernatowicz, P. et al. A 13C, 15N and 77Se NMR study of some seleno and diseleno azines and related compounds. Pol. J. Chem. 71, 441–445 (1997).
Pacuła, A. J., Ścianowski, J. & Aleksandrzak, K. B. Highly efficient synthesis and antioxidant capacity of N-substituted benzisoselenazol-3(2H)-ones. RSC Adv. 4(90), 48959–48962 (2014).
Kasprzyk, R. et al. Direct high-throughput screening assay for mRNA cap guanine-N7 methyltransferase activity. Chemistry 26(49), 11266–11275 (2020).
Delgado-Roche, L. & Mesta, F. Oxidative stress as key player in severe acute respiratory syndrome coronavirus (SARS-CoV) infection. Arch. Med. Res. 51(5), 384–387 (2020).
Takayama, K. In vitro and animal models for SARS-CoV-2 research. Trends Pharmacol. Sci. 41(8), 513–517 (2020).
Menendez, C. A. et al. Molecular characterization of ebselen binding activity to SARS-CoV-2 main protease. Sci. Adv. 6(37), eabd0345 (2020).
Qiao, Z. et al. The Mpro structure-based modifications of ebselen derivatives for improved antiviral activity against SARS-CoV-2 virus. Bioorg. Chem. 117, 105455 (2021).
Ma, C. et al. Ebselen, disulfiram, carmofur, PX-12, tideglusib, and shikonin are nonspecific promiscuous SARS-CoV-2 main protease inhibitors. ACS Pharmacol. Transl. Sci. 3(6), 1265–1277 (2020).
Ma, C. et al. Validation and invalidation of SARS-CoV-2 main protease inhibitors using the Flip-GFP and Protease-Glo luciferase assays. Acta Pharm. Sin. B 12(4), 1636–1651 (2022).
Tan, H., Ma, C. & Wang, J. Invalidation of dieckol and 1,2,3,4,6-pentagalloylglucose (PGG) as SARS-CoV-2 main protease inhibitors and the discovery of PGG as a papain-like protease inhibitor. Med. Chem. Res. 31(7), 1147–1153 (2022).
Heilmann, E. et al. A VSV-based assay quantifies coronavirus Mpro/3CLpro/Nsp5 main protease activity and chemical inhibition. Commun. Biol. 5(1), 391 (2022).
Nogueira, C. W., Barbosa, N. V. & Rocha, J. B. T. Toxicology and pharmacology of synthetic organoselenium compounds: An update. Arch. Toxicol. 95(4), 1179–1226 (2021).
Suhail, S. et al. Role of oxidative stress on SARS-CoV (SARS) and SARS-CoV-2 (COVID-19) infection: A review. Protein J. 39(6), 644–656 (2020).
Taylor, E. W. & Radding, W. Understanding selenium and glutathione as antiviral factors in COVID-19: Does the viral M(pro) protease target host selenoproteins and glutathione synthesis?. Front. Nutr. 7, 143 (2020).
Du, L. et al. Oxidative stress transforms 3CLpro into an insoluble and more active form to promote SARS-CoV-2 replication. Redox. Biol. 48, 102199 (2021).
Lynch, E. & Kil, J. Development of ebselen, a glutathione peroxidase mimic, for the prevention and treatment of noise-induced hearing loss. Semin. Hear. 30(01), 047–055 (2009).
Sharpley, A. L. et al. A phase 2a randomised, double-blind, placebo-controlled, parallel-group, add-on clinical trial of ebselen (SPI-1005) as a novel treatment for mania or hypomania. Psychopharmacology 237(12), 3773–3782 (2020).
Yamaguchi, T. et al. Ebselen in acute ischemic stroke: A placebo-controlled, double-blind clinical trial. Ebselen Study Group. Stroke 29(1), 12–17 (1998).
Singh, N. et al. A safe lithium mimetic for bipolar disorder. Nat. Commun. 4, 1332 (2013).
Granda, J. et al. Synthesis of 7- and 8-functionalized 2-aminophenoxazinones via cyclocondensation of 2-aminophenols. Synthesis 47(21), 3321–3332 (2015).
Welter, A., Christiaens, L. & Wirtz-Peitz, F. Benzisoselenazolones and processes for the treatment of rheumatic and arthritic diseases using them (1983).
Młochowski, J. et al. Aromatic and azaaromatic diselenides, benzisoselenazolones and related compounds as immunomodulators active in humans: Synthesis and properties. Liebigs Ann. Chem. 1993(12), 1239–1244 (1993).
Welter, A. et al. Diselenobis-benzoic acid amides of primary and secondary amines and processes for the treatment of diseases in humans caused by a cell injury (1989).
Kuppers, J. et al. Convergent synthesis of two fluorescent ebselen-coumarin heterodimers. Pharmaceuticals (Basel) 9(3), 43 (2016).
Chang, T. C. et al. Synthesis and biological evaluation of ebselen and its acyclic derivatives. Chem. Pharm. Bull. (Tokyo) 51(12), 1413–1416 (2003).
Gustafsson, T. N. et al. Ebselen and analogs as inhibitors of Bacillus anthracis thioredoxin reductase and bactericidal antibacterials targeting Bacillus species, Staphylococcus aureus and Mycobacterium tuberculosis. Biochim. Biophys. Acta 1860(6), 1265–1271 (2016).
Wan, J. et al. Benzoselenazole ketone compound and application thereof and bactericide (2021).
Bender, C. O. et al. Use of small molecules for the treatment of Clostridium difficile toxicity (2015).
Garland, M. et al. Covalent modifiers of botulinum neurotoxin counteract toxin persistence. ACS Chem. Biol. 14(1), 76–87 (2019).
Xue, X. et al. Production of authentic SARS-CoV M(pro) with enhanced activity: Application as a novel tag-cleavage endopeptidase for protein overproduction. J. Mol. Biol. 366(3), 965–975 (2007).
|
Sources 2/ https://www.nature.com/articles/s41598-023-35907-w The mention sources can contact us to remove/changing this article |
[ad_2]