{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,7]],"date-time":"2026-11-07T22:34:17Z","timestamp":1794090857724,"version":"4.8.0"},"reference-count":55,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["European Journal of Medicinal Chemistry"],"published-print":{"date-parts":[[2023,5]]},"DOI":"10.1016\/j.ejmech.2023.115227","type":"journal-article","created":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T17:19:03Z","timestamp":1677691143000},"page":"115227","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":21,"special_numbering":"C","title":["N-sulfonyl peptide-hybrids as a new class of dengue virus protease inhibitors"],"prefix":"10.1016","volume":"251","author":[{"given":"Somayeh","family":"Behrouz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nikos","family":"K\u00fchl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3522-9182","authenticated-orcid":false,"given":"Christian D.","family":"Klein","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2023.115227_bib1","first-page":"379","article-title":"The dengue viruses","volume":"3","author":"Henchal","year":"1999","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.ejmech.2023.115227_bib2","author":"World Health Organization"},{"key":"10.1016\/j.ejmech.2023.115227_bib3","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/S1473-3099(01)00171-2","article-title":"Dengue: an update","volume":"2","author":"Guzm\u00e1n","year":"2002","journal-title":"Lancet Infect. Dis."},{"key":"10.1016\/j.ejmech.2023.115227_bib4","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1128\/CMR.11.3.480","article-title":"Dengue and dengue hemorrhagic fever","volume":"11","author":"Gubler","year":"1998","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.ejmech.2023.115227_bib5","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1146\/annurev.micro.62.081307.163005","article-title":"Global spread and persistence of dengue","volume":"62","author":"Kyle","year":"2008","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.ejmech.2023.115227_bib6","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1038\/nature12060","article-title":"The global distribution and burden of dengue","volume":"496","author":"Bhatt","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2023.115227_bib7","unstructured":"World Health organization. Dengue guidelines for diagnosis, treatment, prevention and control: New Edition. https:\/\/www.who.int\/rpc\/guidelines\/9789241547871\/en\/ (accessed Mar 31, 2020)."},{"key":"10.1016\/j.ejmech.2023.115227_bib10","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1038\/nrmicro2950","article-title":"West Nile virus infection and immunity","volume":"11","author":"Suthar","year":"2013","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.ejmech.2023.115227_bib11","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.coph.2016.07.015","article-title":"Hepatitis C virus NS3\/4A protease inhibitors","volume":"30","author":"McCauley","year":"2016","journal-title":"Curr. Opin. Pharmacol."},{"key":"10.1016\/j.ejmech.2023.115227_bib12","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/j.ijantimicag.2008.10.010","article-title":"Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV","volume":"33","author":"De Clercq","year":"2009","journal-title":"Int. J. Antimicrob. Agents"},{"key":"10.1016\/j.ejmech.2023.115227_bib13","doi-asserted-by":"crossref","first-page":"11348","DOI":"10.1021\/cr500233q","article-title":"Biochemistry and medicinal chemistry of the dengue virus protease","volume":"114","author":"Nitsche","year":"2014","journal-title":"Chem. Rev."},{"key":"10.1016\/j.ejmech.2023.115227_bib14","doi-asserted-by":"crossref","first-page":"5622","DOI":"10.1021\/acs.jmedchem.5b01653","article-title":"The medicinal chemistry of dengue virus","volume":"59","author":"Behnam","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib15","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1016\/j.antiviral.2013.09.013","article-title":"Ten years of dengue drug discovery: progress and prospects","volume":"100","author":"Lim","year":"2013","journal-title":"Antivir. Res."},{"key":"10.1016\/j.ejmech.2023.115227_bib16","doi-asserted-by":"crossref","first-page":"4448","DOI":"10.1021\/acs.chemrev.7b00719","article-title":"Biochemistry and molecular biology of flaviviruses","volume":"118","author":"Barrows","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.ejmech.2023.115227_bib17","series-title":"In Dengue and Zika: Control and Antiviral Treatment Strategies","first-page":"175","article-title":"Strategies towards protease inhibitors for emerging flaviviruses","author":"Nitsche","year":"2018"},{"key":"10.1016\/j.ejmech.2023.115227_bib18","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1038\/nrd.2017.33","article-title":"Broad-spectrum agents for flaviviral infections: dengue, Zika and beyond","volume":"16","author":"Boldescu","year":"2017","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ejmech.2023.115227_bib19","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.antiviral.2012.02.008","article-title":"Retro peptide-hybrids as selective inhibitors of the dengue virus NS2B-NS3 protease","volume":"94","author":"Nitsche","year":"2012","journal-title":"Antivir. Res."},{"key":"10.1016\/j.ejmech.2023.115227_bib20","doi-asserted-by":"crossref","first-page":"8389","DOI":"10.1021\/jm400828u","article-title":"Thiazolidinone\u2013peptide hybrids as dengue virus protease inhibitors with antiviral activity in cell culture","volume":"56","author":"Nitsche","year":"2013","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib21","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1021\/ml500245v","article-title":"C-Terminal residue optimization and fragment merging: discovery of a potent peptide-hybrid inhibitor of dengue protease","volume":"5","author":"Behnam","year":"2014","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115227_bib22","doi-asserted-by":"crossref","first-page":"9354","DOI":"10.1021\/acs.jmedchem.5b01441","article-title":"Discovery of nanomolar dengue and west nile virus protease inhibitors containing a 4-benzyloxyphenylglycine residue","volume":"58","author":"Behnam","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib23","doi-asserted-by":"crossref","first-page":"7719","DOI":"10.1021\/acs.jmedchem.5b00612","article-title":"Phenylalanine and phenylglycine analogues as arginine mimetics in dengue protease inhibitors","volume":"58","author":"Weigel","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib24","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/S0968-0896(99)00021-8","article-title":"Increased stability of peptidesulfonamide peptidomimetics towards protease catalyzed degradation","volume":"7","author":"de Bont","year":"1999","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib25","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.antiviral.2017.02.014","article-title":"Current therapy for chronic hepatitis C: the role of direct-acting antivirals","volume":"142","author":"Li","year":"2017","journal-title":"Antivir. Res."},{"key":"10.1016\/j.ejmech.2023.115227_bib26","doi-asserted-by":"crossref","first-page":"4156","DOI":"10.1021\/cr608202m","article-title":"Boron containing compounds as protease inhibitors","volume":"112","author":"Smoum","year":"2012","journal-title":"Chem. Rev."},{"key":"10.1016\/j.ejmech.2023.115227_bib27","doi-asserted-by":"crossref","first-page":"1300","DOI":"10.2174\/092986610792231456","article-title":"Synthesis and activity of N-sulfonylamides of tripeptides as potential urokinase inhibitors","volume":"17","author":"Markowska","year":"2010","journal-title":"Protein Pept. Lett."},{"key":"10.1016\/j.ejmech.2023.115227_bib28","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1007\/s10989-012-9338-4","article-title":"Synthesis and biological activity of N-sulfonyltripeptides with C-terminal arginine as potential serine proteases inhibitors","volume":"19","author":"Markowska","year":"2013","journal-title":"Int. J. Pept. Res. Therapeut."},{"key":"10.1016\/j.ejmech.2023.115227_bib29","first-page":"1211","article-title":"Dianhydrohexitole-based benzamidines: an efficient synthesis of new factor Xa inhibitors","volume":"8","author":"Vogler","year":"2004","journal-title":"Synthesis"},{"key":"10.1016\/j.ejmech.2023.115227_bib30","doi-asserted-by":"crossref","first-page":"6370","DOI":"10.1021\/acs.jmedchem.6b00606","article-title":"Optimization of cyclic plasmin inhibitors: from benzamidines to benzylamines","volume":"59","author":"Hinkes","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib31","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/S0960-894X(01)00815-0","article-title":"4-Amidinobenzylamine-based inhibitors of urokinase","volume":"12","author":"K\u00fcnzel","year":"2002","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115227_bib32","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1039\/c2md20074k","article-title":"New 3-amidinophenylalanine-derived inhibitors of matriptase","volume":"3","author":"Hammami","year":"2012","journal-title":"Med. Chem. Commun"},{"key":"10.1016\/j.ejmech.2023.115227_bib33","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1042\/BJ20130101","article-title":"Identification of the first synthetic inhibitors of the type II transmembrane serine protease TMPRSS2 suitable for inhibition of influenza virus activation","volume":"452","author":"Meyer","year":"2013","journal-title":"Biochem. J."},{"key":"10.1016\/j.ejmech.2023.115227_bib34","doi-asserted-by":"crossref","first-page":"3091","DOI":"10.1021\/jm960668h","article-title":"Synthesis and structure-activity relationships of potent thrombin inhibitors: piperazides of 3-amidinophenylalanine","volume":"40","author":"St\u00fcrzebecher","year":"1997","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib35","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1089\/adt.2010.0309","article-title":"Virtual ligand screening of the national cancer institute (NCI) compound library leads to the allosteric inhibitory scaffolds of the west nile virus ns3 proteinase","volume":"9","author":"Shiryaev","year":"2011","journal-title":"Assay Drug Dev. Technol."},{"key":"10.1016\/j.ejmech.2023.115227_bib36","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.bioorg.2015.07.005","article-title":"Synthesis and molecular modelling studies of novel sulphonamide derivatives as dengue virus 2 protease inhibitors","volume":"62","author":"Timiri","year":"2015","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib37","doi-asserted-by":"crossref","first-page":"6389","DOI":"10.2147\/DDDT.S94207","article-title":"Identification of covalent active site inhibitors of dengue virus protease","volume":"9","author":"Koh-Stenta","year":"2015","journal-title":"Drug Des. Dev. Ther."},{"key":"10.1016\/j.ejmech.2023.115227_bib38","doi-asserted-by":"crossref","first-page":"2325","DOI":"10.1016\/j.tetlet.2017.04.047","article-title":"Phenylglycine racemization in Fmoc-based solid-phase peptide synthesis: stereochemical stability is achieved by choice of reaction conditions","volume":"58","author":"Liang","year":"2017","journal-title":"Tetrahedron Lett."},{"key":"10.1016\/j.ejmech.2023.115227_bib39","doi-asserted-by":"crossref","first-page":"3587","DOI":"10.1039\/B606875H","article-title":"Synthesis and structural investigations of N-alkylated \u03b2-peptidosulfonamide\u2013peptide hybrids of the amyloidogenic amylin(20\u201329) sequence: implications of supramolecular folding for the design of peptide-based bionanomaterials","volume":"4","author":"Elgersma","year":"2006","journal-title":"J. Org. Biomol. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib40","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1021\/co300023b","article-title":"Piperazine amide linker for cyclative cleavage from solid support: traceless synthesis of dihydroquinoxalin-2-ones","volume":"14","author":"Neagoie","year":"2012","journal-title":"ACS Comb. Sci."},{"key":"10.1016\/j.ejmech.2023.115227_bib41","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1081\/DMR-120005643","article-title":"Reduction of N-hydroxylated compounds: amidoximes (N-hydroxyamidines) as pro-drugs of amidines","volume":"34","author":"Clement","year":"2002","journal-title":"Drug Metab. Rev."},{"key":"10.1016\/j.ejmech.2023.115227_bib42","doi-asserted-by":"crossref","DOI":"10.1016\/j.tetlet.2021.153342","article-title":"A facile approach towards amidinophenylalanine derivatives as building blocks for the synthesis of non-natural peptides and peptidomimetics","volume":"81","author":"Behrouz","year":"2021","journal-title":"Tetrahedron Lett."},{"key":"10.1016\/j.ejmech.2023.115227_bib43","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1002\/hlca.19530360522","article-title":"Herstellung von \u03b1-Aminos\u00e4ureestern durch Alkoholyse der Methylester","volume":"36","author":"Brenner","year":"1953","journal-title":"Helv. Chim. Acta"},{"key":"10.1016\/j.ejmech.2023.115227_bib44","doi-asserted-by":"crossref","first-page":"8179","DOI":"10.1021\/acs.jmedchem.0c00413","article-title":"A new class of dengue and west nile virus protease inhibitors with submicromolar activity in reporter gene DENV-2 protease and viral replication assays","volume":"63","author":"K\u00fchl","year":"2020","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib45","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1021\/op010204f","article-title":"Large-scale syntheses of Fmoc-protected nonproteogenic amino acids: useful building blocks for combinatorial libraries","volume":"5","author":"Dener","year":"2001","journal-title":"Org. Process Res. Dev."},{"key":"10.1016\/j.ejmech.2023.115227_bib46","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1016\/0022-2836(92)91054-S","article-title":"Refined 2.3\u00c5 X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA: a starting point for improving antithrombotics","volume":"226","author":"Brandstetter","year":"1992","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ejmech.2023.115227_bib47","doi-asserted-by":"crossref","first-page":"3099","DOI":"10.1016\/0006-2952(73)90196-2","article-title":"Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction","volume":"22","author":"Cheng","year":"1973","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.ejmech.2023.115227_bib48","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1177\/1087057108321086","article-title":"A Novel method for determination of the affinity of protein: protein interactions in homogeneous assays","volume":"13","author":"Newton","year":"2008","journal-title":"J. Biomol. Screen"},{"key":"10.1016\/j.ejmech.2023.115227_bib49","doi-asserted-by":"crossref","first-page":"5183","DOI":"10.1021\/jo050477z","article-title":"Convenient synthesis of N-methyl amino acids compatible with Fmoc solid-phase peptide synthesis","volume":"70","author":"Biron","year":"2005","journal-title":"J. Org. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib50","doi-asserted-by":"crossref","first-page":"2301","DOI":"10.1021\/ja9635443","article-title":"Site-selective N-methylation of peptides on solid support","volume":"119","author":"Miller","year":"1997","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2023.115227_bib51","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib52","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1128\/JVI.06225-11","article-title":"Ligand-bound structures of the dengue virus protease reveal the active conformation","volume":"86","author":"Noble","year":"2012","journal-title":"J. Virol."},{"key":"10.1016\/j.ejmech.2023.115227_bib53","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2012a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.ejmech.2023.115227_bib54","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1007\/BF03190489","article-title":"Metabolic assessment in liver microsomes by co-activating cytochrome P450s and UDP-glycosyltransferases","volume":"28","author":"Yan","year":"2003","journal-title":"Eur. J. Drug Metab. Pharmacokinet."},{"key":"10.1016\/j.ejmech.2023.115227_bib55","doi-asserted-by":"crossref","first-page":"1913","DOI":"10.1016\/j.bmcl.2019.05.054","article-title":"Backbone modifications in peptidic inhibitors of flaviviral proteases","volume":"29","author":"Jakob","year":"2019","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2023.115227_bib56","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1385\/MB:33:3:239","article-title":"Methods and protocols of modern solid phase peptide synthesis","volume":"33","author":"Amblard","year":"2006","journal-title":"Mol. Biotechnol."},{"key":"10.1016\/j.ejmech.2023.115227_bib57","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"Automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523423001939?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523423001939?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T14:47:12Z","timestamp":1759330032000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523423001939"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,5]]},"references-count":55,"alternative-id":["S0223523423001939"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2023.115227","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2023,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"N-sulfonyl peptide-hybrids as a new class of dengue virus protease inhibitors","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2023.115227","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"115227"}}