{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,14]],"date-time":"2026-07-14T20:15:38Z","timestamp":1784060138176,"version":"3.55.0"},"reference-count":40,"publisher":"Springer Science and Business Media LLC","issue":"5","license":[{"start":{"date-parts":[[2026,3,4]],"date-time":"2026-03-04T00:00:00Z","timestamp":1772582400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2026,3,4]],"date-time":"2026-03-04T00:00:00Z","timestamp":1772582400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"name":"Centre de recherche en infectiologie porcine et avicole"},{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["RGPIN 06353-2020"],"award-info":[{"award-number":["RGPIN 06353-2020"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008921","name":"Ministry of Agriculture - Saskatchewan","doi-asserted-by":"publisher","award":["20220106"],"award-info":[{"award-number":["20220106"]}],"id":[{"id":"10.13039\/100008921","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Probiotics & Antimicro. Prot."],"published-print":{"date-parts":[[2026,6]]},"DOI":"10.1007\/s12602-025-10870-2","type":"journal-article","created":{"date-parts":[[2026,3,4]],"date-time":"2026-03-04T07:27:59Z","timestamp":1772609279000},"page":"7382-7393","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Total Chemical Synthesis and Evaluation of the Antimicrobial Properties of Porcine \u03b2-Defensin 5 Against Gram-Positive and Gram-Negative Bacteria"],"prefix":"10.1007","volume":"18","author":[{"given":"Arthur Nery","family":"Finatto","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vy","family":"Nguyen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Phuong Trang","family":"Nguyen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steve","family":"Bourgault","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matheus","family":"de Oliveira Costa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,3,4]]},"reference":[{"key":"10870_CR1","doi-asserted-by":"publisher","first-page":"965","DOI":"10.2147\/IDR.S199844","volume":"12","author":"Z Aghapour","year":"2019","unstructured":"Aghapour Z, Gholizadeh P, Ganbarov K et al (2019) Molecular mechanisms related to colistin resistance in Enterobacteriaceae. Infect Drug Resist 12:965\u2013975. https:\/\/doi.org\/10.2147\/IDR.S199844","journal-title":"Infect Drug Resist"},{"key":"10870_CR2","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fpubh.2020.535668","volume":"8","author":"S Dhingra","year":"2020","unstructured":"Dhingra S, Rahman NAA, Peile E et al (2020) Microbial resistance movements: an overview of global public health threats posed by antimicrobial resistance, and how best to counter. Front Public Health 8:1\u201322. https:\/\/doi.org\/10.3389\/fpubh.2020.535668","journal-title":"Front Public Health"},{"key":"10870_CR3","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3402\/dfa.v3i0.18656","volume":"3","author":"RM Neto","year":"2012","unstructured":"Neto RM, Ansaldi MA, da Costa MESM et al (2012) A case report of a multi-drug resistant bacterial infection in a diabetic patient treated in Northeast Brazil. Diabet Foot Ankle 3:1\u20136. https:\/\/doi.org\/10.3402\/dfa.v3i0.18656","journal-title":"Diabet Foot Ankle"},{"key":"10870_CR4","doi-asserted-by":"publisher","first-page":"178","DOI":"10.1016\/j.mjafi.2014.04.011","volume":"71","author":"BAK Jindal","year":"2015","unstructured":"Jindal BAK, Pandya MK, Khan MID (2015) Antimicrobial resistance: a public health challenge. Med J Armed Forces India 71:178\u2013181. https:\/\/doi.org\/10.1016\/j.mjafi.2014.04.011","journal-title":"Med J Armed Forces India"},{"key":"10870_CR5","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41467-019-12364-6","volume":"10","author":"R Spohn","year":"2019","unstructured":"Spohn R, Daruka L, L\u00e1z\u00e1r V et al (2019) Integrated evolutionary analysis reveals antimicrobial peptides with limited resistance. Nat Commun 10:1\u201313. https:\/\/doi.org\/10.1038\/s41467-019-12364-6","journal-title":"Nat Commun"},{"key":"10870_CR6","doi-asserted-by":"publisher","DOI":"10.1126\/science.aau5480","author":"BP Lazzaro","year":"2020","unstructured":"Lazzaro BP, Zasloff M, Rolff J (2020) Antimicrobial peptides: application informed by evolution. Science. https:\/\/doi.org\/10.1126\/science.aau5480","journal-title":"Science"},{"key":"10870_CR7","doi-asserted-by":"publisher","first-page":"386","DOI":"10.1016\/j.molimm.2007.06.001","volume":"45","author":"EJA Veldhuizen","year":"2008","unstructured":"Veldhuizen EJA, Rijnders M, Claassen EA et al (2008) Porcine \u03b2-defensin 2 displays broad antimicrobial activity against pathogenic intestinal bacteria. Mol Immunol 45:386\u2013394. https:\/\/doi.org\/10.1016\/j.molimm.2007.06.001","journal-title":"Mol Immunol"},{"key":"10870_CR8","doi-asserted-by":"publisher","first-page":"280","DOI":"10.1038\/nnano.2010.29","volume":"5","author":"GE Fantner","year":"2010","unstructured":"Fantner GE, Barbero RJ, Gray DS, Belcher AM (2010) Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy. Nat Nanotechnol 5:280\u2013285. https:\/\/doi.org\/10.1038\/nnano.2010.29","journal-title":"Nat Nanotechnol"},{"key":"10870_CR9","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41598-018-32822-3","volume":"8","author":"Rbo Chen","year":"2018","unstructured":"Chen Rbo, Zhang K, Zhang H et al (2018) Analysis of the antimicrobial mechanism of Porcine beta defensin 2 against E. coli by electron microscopy and differentially expressed genes. Sci Rep 8:1\u201314. https:\/\/doi.org\/10.1038\/s41598-018-32822-3","journal-title":"Sci Rep"},{"key":"10870_CR10","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1038\/nrmicro1098","volume":"3","author":"KA Brogden","year":"2005","unstructured":"Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3:238\u2013250. https:\/\/doi.org\/10.1038\/nrmicro1098","journal-title":"Nat Rev Microbiol"},{"key":"10870_CR11","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1128\/AAC.02340-16","volume":"61","author":"C-F Le","year":"2017","unstructured":"Le C-F, Fang C-M, Sekaran SD (2017) Intracellular targeting mechanisms by antimicrobial peptides. Antimicrob Agents Chemother 61:1\u201316. https:\/\/doi.org\/10.1128\/AAC.02340-16","journal-title":"Antimicrob Agents Chemother"},{"key":"10870_CR12","doi-asserted-by":"publisher","first-page":"1","DOI":"10.29219\/fnr.v62.1493","volume":"62","author":"X Dou","year":"2018","unstructured":"Dou X, Han J, Ma Q et al (2018) TLR2\/4-mediated NF-\u03bab pathway combined with the histone modification regulates \u03b2-defensins and interleukins expression by sodium phenyl butyrate in porcine intestinal epithelial cells. Food Nutr Res 62:1\u201313. https:\/\/doi.org\/10.29219\/fnr.v62.1493","journal-title":"Food Nutr Res"},{"key":"10870_CR13","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1186\/s13567-025-01465-4","volume":"56","author":"AN Finatto","year":"2025","unstructured":"Finatto AN, Meurens F, de Oliveira Costa M (2025) Piggybacking on nature: exploring the multifaceted world of Porcine \u03b2-defensins. Vet Res 56:47. https:\/\/doi.org\/10.1186\/s13567-025-01465-4","journal-title":"Vet Res"},{"key":"10870_CR14","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1038\/nrd3591","volume":"11","author":"CD Fjell","year":"2012","unstructured":"Fjell CD, Hiss JA, Hancock REW, Schneider G (2012) Designing antimicrobial peptides: form follows function. Nat Rev Drug Discov 11:37\u201351. https:\/\/doi.org\/10.1038\/nrd3591","journal-title":"Nat Rev Drug Discov"},{"key":"10870_CR15","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2156-13-98","author":"MK Choi","year":"2012","unstructured":"Choi MK, Le MT, Nguyen DT et al (2012) Genome-level identification, gene expression, and comparative analysis of porcine \u03b2-defensin genes. BMC Genet. https:\/\/doi.org\/10.1186\/1471-2156-13-98","journal-title":"BMC Genet"},{"key":"10870_CR16","doi-asserted-by":"publisher","first-page":"105","DOI":"10.4137\/EBO.S25580","volume":"11","author":"J Tu","year":"2015","unstructured":"Tu J, Li D, Li Q et al (2015) Molecular evolutionary analysis of \u03b2-defensin peptides in vertebrates. Evolutionary Bioinformatics 11:105\u2013114. https:\/\/doi.org\/10.4137\/EBO.S25580","journal-title":"Evolutionary Bioinformatics"},{"key":"10870_CR17","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fimmu.2018.03072","volume":"10","author":"KG Meade","year":"2019","unstructured":"Meade KG, O\u2019Farrelly C (2019) \u0392-defensins: farming the Microbiome for homeostasis and health. Front Immunol 10:1\u201320. https:\/\/doi.org\/10.3389\/fimmu.2018.03072","journal-title":"Front Immunol"},{"key":"10870_CR18","doi-asserted-by":"publisher","first-page":"3519","DOI":"10.1002\/ejoc.201402149","volume":"2014","author":"TM Postma","year":"2014","unstructured":"Postma TM, Albericio F (2014) Disulfide formation strategies in peptide synthesis. Eur J Org Chem 2014:3519\u20133530. https:\/\/doi.org\/10.1002\/ejoc.201402149","journal-title":"Eur J Org Chem"},{"key":"10870_CR19","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1152\/physiolgenomics.00104.2005","volume":"23","author":"AA Patil","year":"2005","unstructured":"Patil AA, Cai Y, Sang Y et al (2005) Cross-species analysis of the mammalian \u03b2-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. Physiol Genomics 23:5\u201317. https:\/\/doi.org\/10.1152\/physiolgenomics.00104.2005","journal-title":"Physiol Genomics"},{"key":"10870_CR20","doi-asserted-by":"publisher","DOI":"10.1016\/j.addr.2021.05.028","volume":"175","author":"C Wang","year":"2021","unstructured":"Wang C, Hong T, Cui P et al (2021) Antimicrobial peptides towards clinical application: delivery and formulation. Adv Drug Deliv Rev 175:113818. https:\/\/doi.org\/10.1016\/j.addr.2021.05.028","journal-title":"Adv Drug Deliv Rev"},{"key":"10870_CR21","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamem.2020.183273","volume":"1862","author":"C Nehls","year":"2020","unstructured":"Nehls C, B\u00f6hling A, Podschun R et al (2020) Influence of disulfide bonds in human beta defensin-3 on its strain specific activity against Gram-negative bacteria. Biochimica et Biophysica Acta (BBA) - Biomembranes 1862:183273. https:\/\/doi.org\/10.1016\/j.bbamem.2020.183273","journal-title":"Biochimica et Biophysica Acta (BBA) - Biomembranes"},{"key":"10870_CR22","doi-asserted-by":"publisher","first-page":"8880","DOI":"10.1073\/pnas.1533186100","volume":"100","author":"Z Wu","year":"2003","unstructured":"Wu Z, Hoover DM, Yang D et al (2003) Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human \u03b2-defensin 3. Proc Natl Acad Sci U S A 100:8880\u20138885. https:\/\/doi.org\/10.1073\/pnas.1533186100","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10870_CR23","doi-asserted-by":"publisher","first-page":"3349","DOI":"10.1128\/AAC.47.10.3349-3351.2003","volume":"47","author":"G Maisetta","year":"2003","unstructured":"Maisetta G, Batoni G, Esin S et al (2003) Activity of human \u03b2-defensin 3 alone or combined with other antimicrobial agents against oral bacteria. Antimicrob Agents Chemother 47:3349\u20133351. https:\/\/doi.org\/10.1128\/AAC.47.10.3349-3351.2003","journal-title":"Antimicrob Agents Chemother"},{"key":"10870_CR24","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1002\/bip.20193","volume":"80","author":"A Schulz","year":"2005","unstructured":"Schulz A, Kl\u00fcver E, Schulz-Maronde S, Adermann K (2005) Engineering disulfide bonds of the novel human \u03b2\u2010defensins hBD\u201027 and hBD\u201028: differences in disulfide formation and biological activity among human \u03b2\u2010defensins. Pept Sci 80:34\u201349. https:\/\/doi.org\/10.1002\/bip.20193","journal-title":"Pept Sci"},{"key":"10870_CR25","doi-asserted-by":"publisher","DOI":"10.3390\/ijms232012562","author":"A Walewska","year":"2022","unstructured":"Walewska A, Kosikowska-Adamus P, Tomczykowska M et al (2022) Improving Fmoc solid phase synthesis of human beta defensin 3. Int J Mol Sci. https:\/\/doi.org\/10.3390\/ijms232012562","journal-title":"Int J Mol Sci"},{"key":"10870_CR26","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1007\/s10989-006-9018-3","volume":"12","author":"N Chino","year":"2006","unstructured":"Chino N, Kubo S, Nishio H et al (2006) Chemical synthesis of human \u03b2-defensin (hBD)-1, -2, -3 and \u2013 4: optimization of the oxidative folding reaction. Int J Pept Res Ther 12:203\u2013209. https:\/\/doi.org\/10.1007\/s10989-006-9018-3","journal-title":"Int J Pept Res Ther"},{"key":"10870_CR27","doi-asserted-by":"publisher","first-page":"878","DOI":"10.1021\/ol203407z","volume":"14","author":"AM Heapy","year":"2012","unstructured":"Heapy AM, Williams GM, Fraser JD, Brimble MA (2012) Synthesis of a dicarba analogue of human \u03b2-defensin-1 using a combined ring closing metathesis - Native chemical ligation strategy. Org Lett 14:878\u2013881. https:\/\/doi.org\/10.1021\/ol203407z","journal-title":"Org Lett"},{"key":"10870_CR28","doi-asserted-by":"publisher","first-page":"7568","DOI":"10.1038\/s41598-025-90688-8","volume":"15","author":"AN Finatto","year":"2025","unstructured":"Finatto AN, Yang C, de Oliveira Costa M (2025) Porcine \u03b2-defensin 5 (pBD-5) modulates the inflammatory and metabolic host intestinal response to infection. Sci Rep 15:7568. https:\/\/doi.org\/10.1038\/s41598-025-90688-8","journal-title":"Sci Rep"},{"key":"10870_CR29","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","volume":"596","author":"J Jumper","year":"2021","unstructured":"Jumper J, Evans R, Pritzel A et al (2021) Highly accurate protein structure prediction with alphafold. Nature 596:583\u2013589. https:\/\/doi.org\/10.1038\/s41586-021-03819-2","journal-title":"Nature"},{"key":"10870_CR30","doi-asserted-by":"publisher","first-page":"243","DOI":"10.1002\/psc.749","volume":"12","author":"E Kl\u00fcver","year":"2006","unstructured":"Kl\u00fcver E, Adermann K, Schulz A (2006) Synthesis and structure-activity relationships of \u03b2-defensins, multi-functional peptides of the immune system. J Pept Sci 12:243\u2013257. https:\/\/doi.org\/10.1002\/psc.749","journal-title":"J Pept Sci"},{"key":"10870_CR31","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1007\/s10989-019-09837-z","volume":"26","author":"Y Ma","year":"2020","unstructured":"Ma Y, Kim SS, Maeng CH et al (2020) Key role of disulfide bridges in the antimicrobial activity of Beta-Defensin from olive flounder. Int J Pept Res Ther 26:291\u2013299. https:\/\/doi.org\/10.1007\/s10989-019-09837-z","journal-title":"Int J Pept Res Ther"},{"key":"10870_CR32","doi-asserted-by":"publisher","first-page":"2338","DOI":"10.1128\/IAI.74.4.2338-2352.2006","volume":"74","author":"S Elahi","year":"2006","unstructured":"Elahi S, Buchanan RM, Attah-Poku S et al (2006) The host defense peptide beta-defensin 1 confers protection against Bordetella pertussis in newborn piglets. Infect Immun 74:2338\u20132352. https:\/\/doi.org\/10.1128\/IAI.74.4.2338-2352.2006","journal-title":"Infect Immun"},{"key":"10870_CR33","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41598-017-18102-6","volume":"7","author":"S Sinha","year":"2017","unstructured":"Sinha S, Zheng L, Mu Y et al (2017) Structure and interactions of a host defense antimicrobial peptide Thanatin in lipopolysaccharide micelles reveal mechanism of bacterial cell agglutination. Sci Rep 7:1\u201313. https:\/\/doi.org\/10.1038\/s41598-017-18102-6","journal-title":"Sci Rep"},{"key":"10870_CR34","doi-asserted-by":"publisher","first-page":"2378","DOI":"10.1128\/AAC.06107-11","volume":"56","author":"D Pulido","year":"2012","unstructured":"Pulido D, Moussaoui M, Andreu D et al (2012) Antimicrobial action and cell agglutination by the eosinophil cationic protein are modulated by the cell wall lipopolysaccharide structure. Antimicrob Agents Chemother 56:2378\u20132385. https:\/\/doi.org\/10.1128\/AAC.06107-11","journal-title":"Antimicrob Agents Chemother"},{"key":"10870_CR35","doi-asserted-by":"publisher","first-page":"1878","DOI":"10.1172\/JCI28422","volume":"116","author":"OE S\u00f8rensen","year":"2006","unstructured":"S\u00f8rensen OE, Thapa DR, Roup\u00e9 KM et al (2006) Injury-induced innate immune response in human skin mediated by transactivation of the epidermal growth factor receptor. J Clin Invest 116:1878\u20131885. https:\/\/doi.org\/10.1172\/JCI28422","journal-title":"J Clin Invest"},{"key":"10870_CR36","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s40168-024-01859-0","volume":"12","author":"P Koleva","year":"2024","unstructured":"Koleva P, He J, Dunsmore G et al (2024) CD71\u2009+\u2009erythroid cells promote intestinal symbiotic microbial communities in pregnancy and neonatal period. Microbiome 12:1\u201323. https:\/\/doi.org\/10.1186\/s40168-024-01859-0","journal-title":"Microbiome"},{"key":"10870_CR37","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fmicb.2020.00103","volume":"11","author":"B El Shazely","year":"2020","unstructured":"El Shazely B, Yu G, Johnston PR, Rolff J (2020) Resistance evolution against antimicrobial peptides in Staphylococcus aureus alters pharmacodynamics beyond the MIC. Front Microbiol 11:1\u201311. https:\/\/doi.org\/10.3389\/fmicb.2020.00103","journal-title":"Front Microbiol"},{"key":"10870_CR38","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fmicb.2020.593215","volume":"11","author":"L Assoni","year":"2020","unstructured":"Assoni L, Milani B, Carvalho MR et al (2020) Resistance mechanisms to antimicrobial peptides in Gram-Positive bacteria. Front Microbiol 11:1\u201320. https:\/\/doi.org\/10.3389\/fmicb.2020.593215","journal-title":"Front Microbiol"},{"key":"10870_CR39","doi-asserted-by":"publisher","first-page":"5134","DOI":"10.1128\/AAC.00780-13","volume":"57","author":"T Shireen","year":"2013","unstructured":"Shireen T, Singh M, Das T, Mukhopadhyay K (2013) Differential adaptive responses of Staphylococcus aureus to in vitro selection with different antimicrobial peptides. Antimicrob Agents Chemother 57:5134\u20135137. https:\/\/doi.org\/10.1128\/AAC.00780-13","journal-title":"Antimicrob Agents Chemother"},{"key":"10870_CR40","doi-asserted-by":"publisher","DOI":"10.1128\/microbiolspec.VMBF-0006-2015","author":"JN Cole","year":"2016","unstructured":"Cole JN, Nizet V (2016) Bacterial evasion of host antimicrobial peptide defenses. Microbiol Spectr. https:\/\/doi.org\/10.1128\/microbiolspec.VMBF-0006-2015","journal-title":"Microbiol Spectr"}],"container-title":["Probiotics and Antimicrobial Proteins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12602-025-10870-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12602-025-10870-2","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12602-025-10870-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,14]],"date-time":"2026-07-14T20:02:20Z","timestamp":1784059340000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s12602-025-10870-2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,3,4]]},"references-count":40,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2026,6]]}},"alternative-id":["10870"],"URL":"https:\/\/doi.org\/10.1007\/s12602-025-10870-2","relation":{},"ISSN":["1867-1306","1867-1314"],"issn-type":[{"value":"1867-1306","type":"print"},{"value":"1867-1314","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,3,4]]},"assertion":[{"value":"30 May 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"26 November 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 March 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"This study did not involve human participants, use of human biological materials, or multidrug-resistant microorganisms. The blood used in the experiments was porcine, commercially sourced from a certified laboratory, and not collected specifically for this study. As such, ethical approval was not required under institutional or national guidelines.","order":1,"name":"Ethics","label":"Ethical Approval","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","label":"Competing Interests","group":{"name":"EthicsHeading","label":"Declarations"}}]}}