{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,12]],"date-time":"2026-06-12T12:18:31Z","timestamp":1781266711035,"version":"3.54.1"},"reference-count":58,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2023,4,28]],"date-time":"2023-04-28T00:00:00Z","timestamp":1682640000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Italian Ministry for University and Research (MUR)","award":["PRIN Project 2020833Y75"],"award-info":[{"award-number":["PRIN Project 2020833Y75"]}]},{"name":"Italian Ministry for University and Research (MUR)","award":["PNRR PE-13"],"award-info":[{"award-number":["PNRR PE-13"]}]},{"name":"Italian Ministry for University and Research (MUR)","award":["INF-ACT project"],"award-info":[{"award-number":["INF-ACT project"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>New classes of antibacterial drugs are urgently needed to address the global issue of antibiotic resistance. In this context, peptaibols are promising membrane-active peptides since they are not involved in innate immunity and their antimicrobial activity does not involve specific cellular targets, therefore reducing the chance of bacterial resistance development. Trichogin GA IV is a nonhemolytic, natural, short-length peptaibol active against Gram-positive bacteria and resistant to proteolysis. In this work, we report on the antibacterial activity of cationic trichogin analogs. Several peptides appear non-hemolytic and strongly active against many clinically relevant bacterial species, including antibiotic-resistant clinical isolates, such as Staphylococcus aureus, Acinetobacter baumannii, and extensively drug-resistant Pseudomonas aeruginosa, against which there are only a limited number of antibiotics under development. Our results further highlight how the modification of natural peptides is a valuable strategy for obtaining improved antibacterial agents with potential therapeutic applications.<\/jats:p>","DOI":"10.3390\/ijms24097997","type":"journal-article","created":{"date-parts":[[2023,4,28]],"date-time":"2023-04-28T04:36:15Z","timestamp":1682656575000},"page":"7997","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Peptaibol Analogs Show Potent Antibacterial Activity against Multidrug Resistant Opportunistic Pathogens"],"prefix":"10.3390","volume":"24","author":[{"given":"Chiara","family":"Dalla Torre","sequence":"first","affiliation":[{"name":"Department of Chemical Sciences, University of Padova, Via Marzolo 1, I-35131 Padova, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3001-8159","authenticated-orcid":false,"given":"Filomena","family":"Sannio","sequence":"additional","affiliation":[{"name":"Dipartimento di Biotecnologie Mediche, University of Siena, Viale Bracci 16, I-53100 Siena, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mattia","family":"Battistella","sequence":"additional","affiliation":[{"name":"Department of Chemical Sciences, University of Padova, Via Marzolo 1, I-35131 Padova, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9483-4476","authenticated-orcid":false,"given":"Jean-Denis","family":"Docquier","sequence":"additional","affiliation":[{"name":"Dipartimento di Biotecnologie Mediche, University of Siena, Viale Bracci 16, I-53100 Siena, Italy"},{"name":"Lead Discovery Siena s.r.l., Via Fiorentina 1, I-53100 Siena, Italy"},{"name":"Laboratoire de Bact\u00e9riologie Mol\u00e9culaire, Centre d\u2019Ing\u00e9nierie des Prot\u00e9ines\u2014UR InBioS, University of Li\u00e8ge, All\u00e9e du Six Ao\u00fbt 11, B-4000 Li\u00e8ge, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3302-6499","authenticated-orcid":false,"given":"Marta","family":"De Zotti","sequence":"additional","affiliation":[{"name":"Department of Chemical Sciences, University of Padova, Via Marzolo 1, I-35131 Padova, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,4,28]]},"reference":[{"key":"ref_1","unstructured":"WHO Regional Office for Europe\/European Centre for Disease Prevention and Control (2022). Antimicrobial Resistance Surveillance in Europe 2022\u20132020 Data, WHO Regional Office for Europe."},{"key":"ref_2","unstructured":"Antimicrobial Resistance Collaborators (2022). Global burden of bacterial antimicrobial resistance in 2019: A systematic analysis. Lancet, 399, 629\u2013655."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1038\/s41597-019-0154-y","article-title":"DRAMP 2.0, an updated data repository of antimicrobial peptides","volume":"6","author":"Kang","year":"2019","journal-title":"Sci. Data"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1007\/s10989-021-10325-6","article-title":"A Review of Antimicrobial Peptides: Its Function, Mode of Action and Therapeutic Potential","volume":"28","author":"Nayab","year":"2022","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"668632","DOI":"10.3389\/fcimb.2021.668632","article-title":"Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields","volume":"11","author":"Moretta","year":"2021","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"217","DOI":"10.3389\/fpubh.2014.00217","article-title":"Vancomycin revisited-60 years later","volume":"2","author":"Rubinstein","year":"2014","journal-title":"Front. Public Health"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1128\/CMR.00064-16","article-title":"Polymyxins: Antibacterial activity, susceptibility testing, and resistance mechanisms encoded by plasmids or chromosomes","volume":"30","author":"Poirel","year":"2017","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1038\/nsmb.3439","article-title":"An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome","volume":"24","author":"Florin","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/j.jgar.2020.12.012","article-title":"Proline-rich antimicrobial peptide Api137 is bactericidal in porcine blood infected ex vivo with a porcine or human Klebsiella pneumoniae strain","volume":"24","author":"Krieger","year":"2021","journal-title":"J. Glob. Antimicrob. Resist."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1021\/acschembio.7b00822","article-title":"A peptidomimetic antibiotic interacts with the periplasmic domain of LptD from Pseudomonas aeruginosa","volume":"13","author":"Andolina","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1010","DOI":"10.1126\/science.1182749","article-title":"Peptidomimetic antibiotics target outer-membrane biogenesis in Pseudomonas aeruginosa","volume":"327","author":"Srinivas","year":"2010","journal-title":"Science"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1111\/j.1469-0691.2011.03570.x","article-title":"Multidrug-resistant, extensively drug-resistant and pandrug-resistant bacteria: An international expert proposal for interim standard definitions for acquired resistance","volume":"18","author":"Magiorakos","year":"2012","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"7820","DOI":"10.1039\/D0CS00729C","article-title":"The multifaceted nature of antimicrobial peptides: Current synthetic chemistry approaches and future directions","volume":"50","author":"Gan","year":"2021","journal-title":"Chem. Soc. Rev."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/415389a","article-title":"Antimicrobial peptides of multicellular organisms","volume":"415","author":"Zasloff","year":"2022","journal-title":"Nature"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1038\/35106587","article-title":"Innate antimicrobial peptide protects the skin from invasive bacterial infection","volume":"414","author":"Nizet","year":"2001","journal-title":"Nature"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fmicb.2016.00381","article-title":"Induced bacterial cross-resistance toward host antimicrobial peptides: A worrying phenomenon","volume":"7","author":"Fleitas","year":"2016","journal-title":"Front. Microbiol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1098\/rspb.2005.3301","article-title":"Experimental evolution of resistance to an antimicrobial peptide","volume":"273","author":"Perron","year":"2006","journal-title":"Proc. R. Soc. B."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"4538","DOI":"10.1038\/s41467-019-12364-6","article-title":"Integrated evolutionary analysis reveals antimicrobial peptides with limited resistance","volume":"10","author":"Spohn","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"20","DOI":"10.14715\/cmb\/2017.63.10.4","article-title":"Overview of ribosomal and non-ribosomal antimicrobial peptides produced by Gram positive bacteria","volume":"63","author":"Tajbakhsh","year":"2017","journal-title":"Cell. Mol. Biol."},{"key":"ref_20","unstructured":"Toniolo, C., and Br\u00fcckner, H. (2009). Peptaibiotics: Fungal Peptides containing \u03b1-Dialkyl \u03b1-Amino Acids, Wiley-VCD."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"V\u00edgla\u0161, J., Dobiasov\u00e1, S., Viktorov\u00e1, J., Ruml, T., Repisk\u00e1, V., Olejn\u00edkov\u00e1, P., and Gbelcov\u00e1, H. (2021). Peptaibol-Containing Extracts of Trichoderma atroviride and the Fight against Resistant Microorganisms and Cancer Cells. Molecules, 26.","DOI":"10.3390\/molecules26196025"},{"key":"ref_22","first-page":"E8957","article-title":"Unique Amalgamation of Primary and Secondary Structural Elements Transform Peptaibols into Potent Bioactive Cell-Penetrating Peptides","volume":"114","author":"You","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1656","DOI":"10.1002\/cbic.202000834","article-title":"Insight into the Mechanism of Action and Peptide-Membrane Interactions of Aib-Rich Peptides: Multitechnique Experimental and Theoretical Analysis","volume":"22","author":"Lizio","year":"2021","journal-title":"ChemBioChem"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1263","DOI":"10.1002\/cbdv.200890113","article-title":"Conformational effects on the electron-transfer efficiency in peptide foldamers based on alpha,alpha-disubstituted glycyl residues","volume":"5","author":"Gatto","year":"2008","journal-title":"Chem. Biodivers."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1002\/cbdv.201200427","article-title":"The comprehensive peptaibiotics database","volume":"10","author":"Stoppacher","year":"2013","journal-title":"Chem. Biodivers."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2170","DOI":"10.1021\/ja00032a035","article-title":"Trichogin A IV, an 11-residue lipopeptaibol from Trichoderma longibrachiatum","volume":"114","author":"Rebuffat","year":"1992","journal-title":"J. Am. Chem. Soc."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1002\/psc.500","article-title":"Trichogin: A paradigm for lipopeptaibols","volume":"9","author":"Peggion","year":"2003","journal-title":"J. Pept. Sci."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1007\/PL00000932","article-title":"Lipopeptaibols, a novel family of membrane active, antimicrobial peptides","volume":"58","author":"Toniolo","year":"2001","journal-title":"Cell Mol. Life Sci."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Sood, M., Kapoor, D., Kumar, V., Sheteiwy, M.S., Ramakrishnan, M., Landi, M., Araniti, F., and Sharma, A. (2020). Trichoderma: The \u201cSecrets\u201d of a Multitalented Biocontrol Agent. Plants, 9.","DOI":"10.3390\/plants9060762"},{"key":"ref_30","first-page":"109","article-title":"Trichoderma as Potential Biocontrol Agent, Its Exploitation in Agriculture: A Review","volume":"2","author":"Ghazanfar","year":"2018","journal-title":"Plant Prot."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1002\/psc.1135","article-title":"Trichogin GA IV: An antibacterial and protease-resistant peptide","volume":"15","author":"Biondi","year":"2009","journal-title":"J. Pept. Sci."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"De Zotti, M., Sella, L., Bolzonello, A., Gabbatore, L., Peggion, C., Bortolotto, A., Elmaghraby, I., Tundo, S., and Favaron, F. (2020). Targeted Amino Acid Substitutions in a Trichoderma Peptaibol Confer Activity against Fungal Plant Pathogens and Protect Host Tissues from Botrytis Cinerea Infection. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21207521"},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Bolzonello, A., Morbiato, L., Tundo, S., Sella, L., Baccelli, I., Echeverrigaray, S., Musetti, R., De Zotti, M., and Favaron, F. (2023). Peptide analogs of a Trichoderma peptaibol effectively control downy mildew in the vineyard. Plant Dis., advance online publication.","DOI":"10.1094\/PDIS-09-22-2064-RE"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"24000","DOI":"10.1038\/srep24000","article-title":"The Rational Search for Selective Anticancer Derivatives of the Peptide Trichogin GA IV: A Multi-Technique Biophysical Approach","volume":"6","author":"Dalzini","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Casagrande, N., Borghese, C., Gabbatore, L., Morbiato, L., De Zotti, M., and Aldinucci, D. (2021). Analogs of a Natural Peptaibol Exert Anticancer Activity in Both Cisplatin- and Doxorubicin-Resistant Cells and in Multicellular Tumor Spheroids. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22168362"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Moret, F., Menilli, L., Milani, C., Di Cintio, G., Dalla Torre, C., Amendola, V., and De Zotti, M. (2023). Anticancer and Targeting Activity of Phytopharmaceutical Structural Analogs of a Natural Peptide from Trichoderma longibrachiatum and Related Peptide-Decorated Gold Nanoparticles. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24065537"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Caracciolo, R., Sella, L., De Zotti, M., Bolzonello, A., Armellin, M., Trainotti, L., Favaron, F., and Tundo, S. (2023). Efficacy of Trichoderma longibrachiatum Trichogin GA IV Peptaibol analogs against the Black Rot Pathogen Xanthomonas campestris pv. campestris and other Phytopathogenic Bacteria. Microorganisms, 11.","DOI":"10.3390\/microorganisms11020480"},{"key":"ref_38","first-page":"1","article-title":"Antimicrobial Resistance in ESKAPE Pathogens","volume":"33","author":"Forde","year":"2020","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"753202","DOI":"10.3389\/fmicb.2021.753202","article-title":"Transcriptomic and Ultrastructural Analyses of Pyricularia oryzae Treated with Fungicidal Peptaibol Analogs of Trichoderma Trichogin","volume":"12","author":"Sella","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"908","DOI":"10.1038\/nsb1294-908","article-title":"Structure determination of racemic trichogin A IV using centrosymmetric crystals","volume":"1","author":"Toniolo","year":"1994","journal-title":"Nat. Struct. Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1039\/C1OB06178J","article-title":"Trichogin GA IV: A versatile template for the synthesis of novel peptaibiotics","volume":"10","author":"Biondi","year":"2012","journal-title":"Org. Biomol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1039\/C9GC03982A","article-title":"Greening Fmoc\/TBu Solid-Phase Peptide Synthesis","volume":"22","author":"Musaimi","year":"2020","journal-title":"Green Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/j.dib.2015.12.006","article-title":"Comparison of bactericidal and cytotoxic activities of trichogin analogs","volume":"6","author":"Tavano","year":"2016","journal-title":"Data Brief"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"iv32","DOI":"10.1093\/jac\/dkz285","article-title":"Characterization of carbapenem-resistant and XDR Pseudomonas aeruginosa in Canada: Results of the CANWARD 2007-16 study","volume":"74","author":"McCracken","year":"2019","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Strateva, T.V., Sirakov, I., Stoeva, T.J., Stratev, A., and Peykov, S. (2023). Phenotypic and Molecular Characteristics of Carbapenem-Resistant Acinetobacter baumannii Isolates from Bulgarian Intensive Care Unit Patients. Microorganisms, 11.","DOI":"10.3390\/microorganisms11040875"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1290","DOI":"10.1093\/cid\/cix893","article-title":"Carbapenemase-Producing Organisms: A Global Scourge","volume":"66","author":"Bonomo","year":"2018","journal-title":"Clin. Infect. Dis."},{"key":"ref_47","unstructured":"Kastin, A.J. (2006). Handbook of Biologically Active Peptides, Academic Press."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1016\/j.bbamem.2006.02.021","article-title":"Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides","volume":"1758","author":"Sato","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1016\/S0006-3495(92)81949-5","article-title":"Protein structures in SDS micelle-protein complexes","volume":"61","author":"Parker","year":"1992","journal-title":"Biophys. J."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0005-2736(99)00200-X","article-title":"Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by \u03b1-helical antimicrobial and cell non-selective membrane-lytic peptides","volume":"1462","author":"Shai","year":"1999","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.bbamem.2014.10.005","article-title":"The peculiar N- and C-termini of trichogin GA IV are needed for membrane interaction and human cell death induction at doses lacking antibiotic activity","volume":"1848","author":"Tavano","year":"2015","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Fasman, G.D. (1996). Circular Dichroism and the Conformational Analysis of Biomolecules, Plenum Press.","DOI":"10.1007\/978-1-4757-2508-7"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"2744","DOI":"10.1021\/ja9537383","article-title":"Circular Dichroism Spectrum of a Peptide 310-Helix","volume":"118","author":"Toniolo","year":"1996","journal-title":"J. Am. Chem. Soc."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1002\/1097-0282(2001)60:6<396::AID-BIP10184>3.0.CO;2-7","article-title":"Control of peptide conformation by the Thorpe-Ingold effect (C alpha-tetrasubstitution)","volume":"60","author":"Toniolo","year":"2001","journal-title":"Biopolymers"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Giamarellou, H., and Karaiskos, I. (2022). Current and Potential Therapeutic Options for Infections Caused by Difficult-to-Treat and Pandrug Resistant Gram-Negative Bacteria in Critically Ill Patients. Antibiotics, 11.","DOI":"10.3390\/antibiotics11081009"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1007\/s11908-018-0629-6","article-title":"Multidrug-Resistant Pseudomonas Infections: Hard to Treat, But Hope on the Horizon?","volume":"20","author":"Nguyen","year":"2018","journal-title":"Curr. Infect. Dis. Rep."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1021\/acs.oprd.6b00439","article-title":"Green Solid-Phase Peptide Synthesis (GSPPS) 3. Green Solvents for Fmoc Removal in Peptide Chemistry","volume":"21","author":"Jad","year":"2017","journal-title":"Org. Process Res. Dev."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.toxicon.2013.09.012","article-title":"Cell-free synthesis of functional thermostable direct hemolysins of Vibrio parahaemolyticus","volume":"76","author":"Bechlars","year":"2013","journal-title":"Toxicon"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/9\/7997\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T19:25:25Z","timestamp":1760124325000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/9\/7997"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,4,28]]},"references-count":58,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2023,5]]}},"alternative-id":["ijms24097997"],"URL":"https:\/\/doi.org\/10.3390\/ijms24097997","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,4,28]]}}}