{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T19:46:31Z","timestamp":1792784791568,"version":"4.5.0"},"reference-count":49,"publisher":"American Chemical Society (ACS)","issue":"10","license":[{"start":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T00:00:00Z","timestamp":1788480000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100006151","name":"Basic Energy Sciences","doi-asserted-by":"publisher","award":["DE-AC02-05CH11231"],"award-info":[{"award-number":["DE-AC02-05CH11231"]}],"id":[{"id":"10.13039\/100006151","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R21AI146542"],"award-info":[{"award-number":["R21AI146542"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100005492","name":"Stanford University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100005492","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["1DP1 AG072438"],"award-info":[{"award-number":["1DP1 AG072438"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Lifespan Research Institute","id":[{"id":"https:\/\/ror.org\/051jvbj60","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Dr. James J. Truchard and the Truchard Foundation"},{"name":"Cisco University Research Program Fund"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,9]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Invasive candidiasis is a serious fungal infection caused by Candida species that can enter the bloodstream and affect major organs, particularly in immunocompromised patients. Development of resistance to standard antifungal therapies, especially with C. auris, has become a major public health issue. While antimicrobial peptides such as the human cathelicidin, LL-37, could represent a possible therapeutic strategy, they are often inactivated when delivered systemically. One alternative therapeutic strategy is antimicrobial peptoids. We studied in vitro activity of three peptoid compounds, oligomers of N-substituted glycines, which mimic the activity of LL-37. Our aim was to establish these peptoid compounds as a potential treatment of invasive candidiasis and compare them to LL-37\u2032s antifungal activity. In vitro, LL-37 did not exhibit antifungal activity (MIC &amp;gt; 64) against all C. auris strains and three species of Candida. In contrast, three peptoids were tested against ten C. auris strains and six other Candida species and showed good activity. MICs measured as low as 4 \u03bcg\/mL for TM5 against C. auris strain 381. Mechanistic studies using TEM and fluorescent confocal microscopy of peptoids against C. auris clinical isolates showed membrane disruption and consolidation of organelles. Peptoids TM4 and TM5 showed strong synergistic effects with fluconazole and caspofungin, and amphotericin B. Serial daily passage of TM4 and TM5 at sub-MIC concentrations showed no resistance developing for up to 3 weeks. Fungicidal kinetics revealed complete killing of fungal colonies after around 1 h. A systemic candidiasis mouse model treated subcutaneously with TM5 3 h after C. auris infection resulted in clearing of infection, indicated by colony forming units (cfu) per gram of kidney, at 24 h with the 5 mg\/kg dose. This demonstrates that antimicrobial peptoids are active systemically and have potential to be an antifungal treatment for candidemia, particularly as an alternative therapy for resistant strains.<\/jats:p>","DOI":"10.1021\/acsinfecdis.6c00525","type":"journal-article","created":{"date-parts":[[2026,9,4]],"date-time":"2026-09-04T21:02:02Z","timestamp":1788555722000},"page":"3462-3471","source":"Crossref","is-referenced-by-count":0,"title":["Antimicrobial\nPeptoids Show Potent Antifungal Activity\nagainst\n                    <i>Candidozyma (Candida) auris In Vivo<\/i>\n                    and Broad-Spectrum\nActivity\n                    <i>In Vitro<\/i>\n                    against Other\n                    <i>Candida<\/i>\n                    Species"],"prefix":"10.1021","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6422-7720","authenticated-orcid":true,"given":"Lisa K.","family":"Ryan","sequence":"first","affiliation":[{"name":"University of Louisville Center for Predictive Medicine , , ,","place":["Louisville, Kentucky, United States, 40202"]},{"name":"University of Louisville School of Dentistry , , , ,","place":["Louisville, Kentucky, United States, 40202"]},{"name":"University of Florida College of Medicine , , , ,","place":["Gainesville, Florida, United States, 32608"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabella M.","family":"Griffiths","sequence":"additional","affiliation":[{"name":"University of Louisville School of Dentistry , , , ,","place":["Louisville, Kentucky, United States, 40202"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Uyen Emily","family":"Do","sequence":"additional","affiliation":[{"name":"University of Louisville School of Dentistry , , , ,","place":["Louisville, Kentucky, United States, 40202"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3765-5791","authenticated-orcid":true,"given":"Denny","family":"Gao","sequence":"additional","affiliation":[{"name":"University of Louisville School of Dentistry , , , ,","place":["Louisville, Kentucky, United States, 40202"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erika L.","family":"Figgins","sequence":"additional","affiliation":[{"name":"University of Louisville School of Dentistry , , , ,","place":["Louisville, Kentucky, United States, 40202"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0000-4400-8715","authenticated-orcid":true,"given":"Kristian","family":"S\u00f8rensen","sequence":"additional","affiliation":[{"name":"Stanford University Schools of Medicine and Engineering , , , ,","place":["Stanford, California, United States, 94305"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9169-7410","authenticated-orcid":true,"given":"Jennifer S.","family":"Lin","sequence":"additional","affiliation":[{"name":"Stanford University Schools of Medicine and Engineering , , , ,","place":["Stanford, California, United States, 94305"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7643-4508","authenticated-orcid":true,"given":"Natalia","family":"Molchanova","sequence":"additional","affiliation":[{"name":"Stanford University Schools of Medicine and Engineering , , , ,","place":["Stanford, California, United States, 94305"]},{"name":"Lawrence Berkeley National Laboratory , , , ,","place":["Berkeley, California, United States, 94720"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kent","family":"Kirshenbaum","sequence":"additional","affiliation":[{"name":"New York University , , , ,","place":["New York, New York, United States, 10003"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0735-6873","authenticated-orcid":true,"given":"Annelise E.","family":"Barron","sequence":"additional","affiliation":[{"name":"Stanford University Schools of Medicine and Engineering , , , ,","place":["Stanford, California, United States, 94305"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3596-9773","authenticated-orcid":true,"given":"Gill","family":"Diamond","sequence":"additional","affiliation":[{"name":"University of Louisville Center for Predictive Medicine , , ,","place":["Louisville, Kentucky, United States, 40202"]},{"name":"University of Louisville School of Dentistry , , , ,","place":["Louisville, Kentucky, United States, 40202"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,4]]},"reference":[{"issue":"7","key":"2026100909094987700_cit1","doi-asserted-by":"publisher","first-page":"e428","DOI":"10.1016\/S1473-3099(23)00692-8","article-title":"Global\nincidence and mortality of severe fungal disease","volume":"24","author":"Denning","year":"2024","journal-title":"Lancet Infect Dis"},{"key":"2026100909094987700_cit2","doi-asserted-by":"publisher","DOI":"10.3389\/fcimb.2025.1641373","article-title":"Innovative\nantifungal strategies\nto combat drug-resistant Candida auris: recent advances\nand clinical implications","volume":"15","author":"Du","year":"2025","journal-title":"Frontiers in Cell\nand Infect Microbiol"},{"key":"2026100909094987700_cit3","unstructured":"CDC.\n          .  Centers for Diseaes Control Candida auris\nTracker. 2026. https:\/\/www.cdc.gov\/candida-auris\/tracking-c-auris\/index.html (accessed 3-19-26)."},{"key":"2026100909094987700_cit4","doi-asserted-by":"publisher","first-page":"1722","DOI":"10.3390\/encyclopedia2040118","article-title":"Antifungals and drug\nresistance","volume":"2","author":"Hossain","year":"2022","journal-title":"Encyclopedia"},{"issue":"suppl_3","key":"2026100909094987700_cit5","doi-asserted-by":"publisher","first-page":"S445","DOI":"10.1093\/infdis\/jix131","article-title":"Multidrug-resistant\ncandida: Epidemiology, molecular\nmechanisms, and treatment","volume":"216","author":"Arendrup","year":"2017","journal-title":"J. Infect Dis"},{"issue":"32","key":"2026100909094987700_cit6","doi-asserted-by":"publisher","first-page":"20438","DOI":"10.1074\/jbc.273.32.20438","article-title":"Candidacidal activity of salivary histatins. Identification\nof a histatin 5-binding protein on Candida albicans","volume":"273","author":"Edgerton","year":"1998","journal-title":"J. Biol. Chem."},{"issue":"5","key":"2026100909094987700_cit7","doi-asserted-by":"publisher","first-page":"445","DOI":"10.1177\/154405910508400509","article-title":"Human beta-defensins:\ndifferential activity against\ncandidal species and regulation by Candida albicans","volume":"84","author":"Feng","year":"2005","journal-title":"J. Dent Res."},{"issue":"6","key":"2026100909094987700_cit8","doi-asserted-by":"publisher","first-page":"1829","DOI":"10.1172\/JCI113527","article-title":"Modulation of the\nin vitro candidacidal activity of human neutrophil defensins by target\ncell metabolism and divalent cations","volume":"81","author":"Lehrer","year":"1988","journal-title":"J. Clin\nInvest"},{"issue":"1","key":"2026100909094987700_cit9","doi-asserted-by":"publisher","first-page":"154","DOI":"10.1128\/AAC.00478-06","article-title":"Human beta-defensins\nkill Candida albicans in an energy-dependent and\nsalt-sensitive manner without causing membrane disruption","volume":"51","author":"Vylkova","year":"2007","journal-title":"Antimicrob. Agents Chemother."},{"issue":"9","key":"2026100909094987700_cit10","doi-asserted-by":"publisher","first-page":"2256","DOI":"10.1128\/AAC.43.9.2256","article-title":"Histatin\n3-mediated killing of Candida albicans: effect of\nextracellular salt concentration on binding and internalization","volume":"43","author":"Xu","year":"1999","journal-title":"Antimicrob. Agents Chemother."},{"issue":"2","key":"2026100909094987700_cit11","doi-asserted-by":"publisher","first-page":"e01872","DOI":"10.1128\/AAC.01872-17","article-title":"Fluconazole-resistant Candida auris is susceptible to salivary histatin 5 killing\nand to intrinsic host defenses","volume":"62","author":"Pathirana","year":"2018","journal-title":"Antimicrob.\nAgents Chemother."},{"issue":"5","key":"2026100909094987700_cit12","doi-asserted-by":"publisher","DOI":"10.1099\/jmm.0.001835","article-title":"Antifungal\nactivity of human antimicrobial\npeptides targeting apoptosis in Candida auris","volume":"73","author":"Shaban","year":"2024","journal-title":"J. Med. Microbiol"},{"issue":"3","key":"2026100909094987700_cit13","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0017755","article-title":"Human antimicrobial\npeptide LL-37 inhibits adhesion of Candida albicans by interacting with yeast cell-wall carbohydrates","volume":"6","author":"Tsai","year":"2011","journal-title":"PLoS One"},{"issue":"4","key":"2026100909094987700_cit14","doi-asserted-by":"publisher","first-page":"241","DOI":"10.3390\/jof6040241","article-title":"Host defense peptides\nas templates for antifungal drug development","volume":"6","author":"Basso","year":"2020","journal-title":"J. Fungi (Basel)"},{"issue":"3","key":"2026100909094987700_cit15","doi-asserted-by":"publisher","first-page":"366","DOI":"10.3390\/ph8030366","article-title":"Peptides and peptidomimetics for antimicrobial drug\ndesign","volume":"8","author":"Mojsoska","year":"2015","journal-title":"Pharmaceuticals (Basel)"},{"key":"2026100909094987700_cit16","doi-asserted-by":"publisher","first-page":"10646","DOI":"10.1021\/ja00052a076","article-title":"Efficient method\nfor the preparation of peptoids [oligo(N-substituted glycines)] by\nsubmonomer solid-phase synthesis","volume":"114","author":"Zuckermann","year":"1992","journal-title":"J. Am. Chem.\nSoc."},{"key":"2026100909094987700_cit17","doi-asserted-by":"publisher","first-page":"20","DOI":"10.1002\/ddr.430350105","article-title":"Comparison of the proteolytic susceptibilites\nof homologous L-amino acid, D-amino acid, and N-substituted glycine\npeptide and peptoid oligomers","volume":"35","author":"Miller","year":"1995","journal-title":"Drug Dev. Res."},{"issue":"8","key":"2026100909094987700_cit18","doi-asserted-by":"publisher","first-page":"2794","DOI":"10.1073\/pnas.0708254105","article-title":"Peptoids that mimic\nthe structure, function, and mechanism of helical antimicrobial peptides","volume":"105","author":"Chongsiriwatana","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"1","key":"2026100909094987700_cit19","doi-asserted-by":"publisher","first-page":"1033","DOI":"10.1038\/s42003-024-06725-1","article-title":"Peptide-mimetic\ntreatment of Pseudomonas aeruginosa in a mouse model\nof respiratory infection","volume":"7","author":"Moule","year":"2024","journal-title":"Commun. Biol."},{"issue":"3","key":"2026100909094987700_cit20","doi-asserted-by":"publisher","DOI":"10.1128\/spectrum.00534-22","article-title":"Efficacy\nof cathelicidin-mimetic\nantimicrobial peptoids against Staphylococcus aureus","volume":"10","author":"Benjamin","year":"2022","journal-title":"Microbiol Spectr"},{"issue":"6","key":"2026100909094987700_cit21","doi-asserted-by":"publisher","first-page":"3058","DOI":"10.1128\/AAC.01667-10","article-title":"Efficacy of antimicrobial\npeptoids against Mycobacterium tuberculosis","volume":"55","author":"Kapoor","year":"2011","journal-title":"Antimicrob.\nAgents Chemother."},{"issue":"10","key":"2026100909094987700_cit22","doi-asserted-by":"crossref","DOI":"10.1099\/mic.0.001607","article-title":"Antiparasitic\neffect of peptoids against Cryptosporidium parvum","volume":"171","author":"Lamont","year":"2025","journal-title":"Microbiology (Reading)"},{"issue":"11","key":"2026100909094987700_cit23","doi-asserted-by":"publisher","first-page":"5399","DOI":"10.1128\/AAC.00578-11","article-title":"Functional synergy between antimicrobial\npeptoids and peptides against Gram-negative bacteria","volume":"55","author":"Chongsiriwatana","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"2026100909094987700_cit24","doi-asserted-by":"publisher","DOI":"10.1038\/srep42332","article-title":"Peptoids successfully\ninhibit the growth of Gram negative E. coli causing\nsubstantial membrane damage","volume":"7","author":"Mojsoska","year":"2017","journal-title":"Sci. Rep"},{"issue":"6","key":"2026100909094987700_cit25","doi-asserted-by":"publisher","first-page":"3054","DOI":"10.1128\/AAC.01516-10","article-title":"Antimicrobial peptoids\nare effective\nagainst Pseudomonas aeruginosa biofilms","volume":"55","author":"Kapoor","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"issue":"4","key":"2026100909094987700_cit26","doi-asserted-by":"publisher","first-page":"304","DOI":"10.3390\/ph14040304","article-title":"Potent antiviral\nactivity against HSV-1 and SARS-CoV-2 by antimicrobial peptoids","volume":"14","author":"Diamond","year":"2021","journal-title":"Pharmaceuticals (Basel)"},{"issue":"4","key":"2026100909094987700_cit27","doi-asserted-by":"publisher","first-page":"464","DOI":"10.3390\/pharmaceutics16040464","article-title":"Antiviral effect of antimicrobial\npeptoid TM9 and murine model of respiratory coronavirus infection","volume":"16","author":"Lebedev","year":"2024","journal-title":"Pharmaceutics"},{"issue":"8","key":"2026100909094987700_cit28","doi-asserted-by":"publisher","first-page":"1508","DOI":"10.1021\/acsinfecdis.3c00063","article-title":"Peptidomimetic\noligomers targeting membrane phosphatidylserine exhibit broad antiviral\nactivity","volume":"9","author":"Tate","year":"2023","journal-title":"ACS Infect Dis"},{"issue":"1","key":"2026100909094987700_cit29","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-017-16180-0","article-title":"Intracellular biomass\nflocculation as a key mechanism of rapid bacterial killing by cationic,\namphipathic antimicrobial peptides and peptoids","volume":"7","author":"Chongsiriwatana","year":"2017","journal-title":"Sci. Rep"},{"issue":"46","key":"2026100909094987700_cit30","doi-asserted-by":"publisher","first-page":"19375","DOI":"10.1073\/pnas.0906145106","article-title":"Soft X-ray\ntomography\nof phenotypic switching and the cellular response to antifungal peptoids\nin Candida albicans","volume":"106","author":"Uchida","year":"2009","journal-title":"Proc.\nNatl. Acad. Sci. U. S. A."},{"issue":"27","key":"2026100909094987700_cit31","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2535920123","article-title":"Antimicrobial peptoids\npass rapidly\nthrough bacterial membranes and flocculate ribosomes and DNA: A single-cell\nfluorescence study","volume":"123","author":"Zhu","year":"2026","journal-title":"Proc. Natl. Acad. Sci. U.\nS. A."},{"issue":"5","key":"2026100909094987700_cit32","doi-asserted-by":"publisher","first-page":"370","DOI":"10.3390\/jof11050370","article-title":"Evaluation\nof the synergistic activity of antimicrobial peptidomimetics or colistin\nsulphate with conventional antifungals against yeasts of medical importance","volume":"11","author":"Mishra","year":"2025","journal-title":"J. Fungi (Basel)"},{"issue":"3","key":"2026100909094987700_cit33","doi-asserted-by":"publisher","DOI":"10.1093\/jambio\/lxaf031","article-title":"Antimicrobial activity of peptoids\nagainst Metallo-beta-lactamase-producing Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and other\nWHO priority pathogens, including Candida auris","volume":"136","author":"Mishra","year":"2025","journal-title":"J. Appl. Microbiol."},{"issue":"7","key":"2026100909094987700_cit34","doi-asserted-by":"publisher","first-page":"1323","DOI":"10.1021\/acsmedchemlett.5c00200","article-title":"Structural optimization\nof antifungal peptoids targeting Candida albicans","volume":"16","author":"Tran","year":"2025","journal-title":"ACS medicinal chemistry\nletters"},{"issue":"1","key":"2026100909094987700_cit35","doi-asserted-by":"publisher","first-page":"4353","DOI":"10.1038\/s41598-017-04462-6","article-title":"Potent in\nvitro and in vivo antifungal activity of a small molecule host defense\npeptide mimic through a membrane-active mechanism","volume":"7","author":"Menzel","year":"2017","journal-title":"Sci. Rep"},{"key":"2026100909094987700_cit36","doi-asserted-by":"publisher","first-page":"2703","DOI":"10.1021\/acsinfecdis.6c00224","article-title":"In Vivo Activity of\nAntimicrobial\nPeptoid Oligomers against HSV-1 in a Mouse Model of Herpes Labialis","volume":"12","author":"Figgins","year":"2026","journal-title":"ACS Infect. Dis."},{"issue":"1","key":"2026100909094987700_cit37","doi-asserted-by":"publisher","first-page":"2381","DOI":"10.1038\/s41467-024-46786-8","article-title":"Rapid evolution of\nan adaptive multicellular morphology of Candida auris during systemic infection","volume":"15","author":"Bing","year":"2024","journal-title":"Nat. Commun."},{"issue":"3","key":"2026100909094987700_cit38","doi-asserted-by":"publisher","first-page":"533","DOI":"10.1021\/acsinfecdis.1c00536","article-title":"Self-assembly\nof antimicrobial peptoids impacts their biological effects on ESKAPE\nbacterial pathogens","volume":"8","author":"Nielsen","year":"2022","journal-title":"ACS Infect Dis"},{"issue":"2","key":"2026100909094987700_cit39","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0135961","article-title":"In vivo,\nin vitro, and in silico characterization of peptoids as antimicrobial\nagents","volume":"11","author":"Czyzewski","year":"2016","journal-title":"PLoS One"},{"key":"2026100909094987700_cit40","doi-asserted-by":"publisher","DOI":"10.1016\/j.bioflm.2025.100272","article-title":"A biofilm-targeting\nlipo-peptoid to treat Pseudomonas aeruginosa and Staphylococcus aureus co-infections","volume":"9","author":"Wardell","year":"2025","journal-title":"Biofilm"},{"issue":"Pt 2","key":"2026100909094987700_cit41","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1042\/BJ20042099","article-title":"Candidacidal\neffects of two antimicrobial peptides: histatin 5 causes small membrane\ndefects, but LL-37 causes massive disruption of the cell membrane","volume":"388","author":"den Hertog","year":"2005","journal-title":"Biochem. J."},{"issue":"6","key":"2026100909094987700_cit42","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0021394","article-title":"Characterizing the\nrole of cell-wall beta-1,3-exoglucanase Xog1p in Candida albicans adhesion by the human antimicrobial peptide LL-37","volume":"6","author":"Tsai","year":"2011","journal-title":"PLoS One"},{"issue":"9","key":"2026100909094987700_cit43","doi-asserted-by":"publisher","first-page":"1823","DOI":"10.1021\/acsinfecdis.2c00288","article-title":"Anti-persister and\nanti-biofilm activity of self-assembled\nantimicrobial peptoid ellipsoidal micelles","volume":"8","author":"Lin","year":"2022","journal-title":"ACS Infect Dis"},{"issue":"6","key":"2026100909094987700_cit44","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0216676","article-title":"Antimicrobial\npeptide LL-37 is bactericidal\nagainst Staphylococcus aureus biofilms","volume":"14","author":"Kang","year":"2019","journal-title":"PLoS One"},{"issue":"1","key":"2026100909094987700_cit45","doi-asserted-by":"publisher","first-page":"30","DOI":"10.3390\/jof4010030","article-title":"Antifungal potential\nof host defense peptide mimetics in a mouse model of disseminated\ncandidiasis","volume":"4","author":"Chowdhury","year":"2018","journal-title":"J. Fungi (Basel)"},{"issue":"7","key":"2026100909094987700_cit46","doi-asserted-by":"publisher","first-page":"3820","DOI":"10.1128\/AAC.02649-13","article-title":"Activity of\npotent and selective\nhost defense peptide mimetics in mouse models of oral candidiasis","volume":"58","author":"Ryan","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"issue":"4","key":"2026100909094987700_cit47","doi-asserted-by":"publisher","first-page":"197","DOI":"10.3390\/jof6040197","article-title":"A novel immunocompetent\nmouse model for testing antifungal\ndrugs against invasive","volume":"6","author":"Ryan","year":"2020","journal-title":"J. Fungi (Basel)"},{"issue":"11","key":"2026100909094987700_cit48","doi-asserted-by":"publisher","first-page":"3973","DOI":"10.1021\/acsinfecdis.4c00681","article-title":"Improved broad spectrum\nantifungal drug synergies with cryptomycin,\na Cdc50-inspired antifungal peptide","volume":"10","author":"Tancer","year":"2024","journal-title":"ACS Infect\nDis"},{"issue":"12","key":"2026100909094987700_cit49","doi-asserted-by":"publisher","DOI":"10.1128\/msphere.00767-25","article-title":"Growth phase influences virulence\nin Candidozyma auris systemic infection models","volume":"10","author":"McFadden","year":"2025","journal-title":"mSphere"}],"container-title":["ACS Infectious Diseases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acsinfecdis.6c00525","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/aidcbc\/article-pdf\/12\/10\/3462\/68393683\/acsinfecdis.6c00525.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/aidcbc\/article-pdf\/12\/10\/3462\/68393683\/acsinfecdis.6c00525.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T13:29:41Z","timestamp":1791552581000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/aidcbc\/article\/12\/10\/3462\/5421757\/Antimicrobial-Peptoids-Show-Potent-Antifungal"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,4]]},"references-count":49,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2026,9,4]]},"published-print":{"date-parts":[[2026,10,9]]}},"URL":"https:\/\/doi.org\/10.1021\/acsinfecdis.6c00525","relation":{},"ISSN":["2373-8227"],"issn-type":[{"value":"2373-8227","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,4]]}}}