{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T19:49:35Z","timestamp":1791229775517,"version":"4.1.0"},"reference-count":76,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2024,11,27]],"date-time":"2024-11-27T00:00:00Z","timestamp":1732665600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2024,11,27]],"date-time":"2024-11-27T00:00:00Z","timestamp":1732665600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31872393"],"award-info":[{"award-number":["31872393"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Commun Biol"],"DOI":"10.1038\/s42003-024-07216-z","type":"journal-article","created":{"date-parts":[[2024,11,27]],"date-time":"2024-11-27T12:19:24Z","timestamp":1732709964000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":25,"title":["An amphipathic peptide combats multidrug-resistant Staphylococcus aureus and biofilms"],"prefix":"10.1038","volume":"7","author":[{"given":"Kun","family":"Zhang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Na","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruoyu","family":"Mao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ya","family":"Hao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Da","family":"Teng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4048-6055","authenticated-orcid":false,"given":"Jianhua","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,11,27]]},"reference":[{"key":"7216_CR1","doi-asserted-by":"publisher","first-page":"135001","DOI":"10.1016\/j.scitotenv.2019.135001","volume":"717","author":"RT Torres","year":"2020","unstructured":"Torres, R. T. et al. Wild boar as a reservoir of antimicrobial resistance. Sci. Total Environ. 717, 135001 (2020).","journal-title":"Sci. Total Environ."},{"key":"7216_CR2","doi-asserted-by":"publisher","first-page":"1329","DOI":"10.1128\/AAC.03937-14","volume":"59","author":"B Deslouches","year":"2014","unstructured":"Deslouches, B., Steckbeck, J. D., Craigo, J. K. & Doi, Y. Engineered cationic antimicrobial peptides to overcome multidrug resistance by ESKAPE pathogens. Antimicrob. Agents. Chemother. 59, 1329\u20131333 (2014).","journal-title":"Antimicrob. Agents. Chemother."},{"key":"7216_CR3","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1080\/22221751.2022.2030196","volume":"11","author":"O Ayobami","year":"2022","unstructured":"Ayobami, O., Brinkwirth, S., Eckmanns, T. & Markwart, R. Antibiotic resistance in hospital-acquired ESCAPE-E infections in low- and lower-middle-income countries: a systematic review and meta-analysis. Emerg. Microbes Infect. 11, 443\u2013451 (2022).","journal-title":"Emerg. Microbes Infect."},{"key":"7216_CR4","doi-asserted-by":"publisher","first-page":"268","DOI":"10.1111\/j.1469-0691.2011.03570.x","volume":"18","author":"AP Magiorakos","year":"2012","unstructured":"Magiorakos, A. P. et al. Multidrug-resistant, extensively drug-resistant and pandrug-resistant bacteria: an international expert proposal for interim standard definitions for acquired resistance. Clin. Microbiol. Infect. 18, 268\u2013281 (2012).","journal-title":"Clin. Microbiol. Infect."},{"key":"7216_CR5","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.drup.2017.03.001","volume":"31","author":"LM Assis","year":"2017","unstructured":"Assis, L. M., Nedeljkovi, M. & Dessen, A. New strategies for targeting and treatment of multi-drug resistant Staphylococcus aureus. Drug Resist. Update 31, 1\u201314 (2017).","journal-title":"Drug Resist. Update"},{"key":"7216_CR6","doi-asserted-by":"publisher","first-page":"831","DOI":"10.1002\/med.21542","volume":"39","author":"J Wang","year":"2018","unstructured":"Wang, J., Dou, X., Song, J., Lyu, Y. & Zhu, X. Antimicrobial peptides: promising alternatives in the post feeding antibiotic era. Med. Res. Rev. 39, 831\u2013859 (2018).","journal-title":"Med. Res. Rev."},{"key":"7216_CR7","doi-asserted-by":"publisher","first-page":"465","DOI":"10.1016\/S0924-8579(03)00180-8","volume":"22","author":"KA Brogden","year":"2003","unstructured":"Brogden, K. A., Ackermann, M. R., Mccray, P. B., Tack, B. F. & Ackermann, M. Antimicrobial peptides in animals and their role in host defences. Int. J. Antimicrob. Agents. 22, 465\u2013478 (2003).","journal-title":"Int. J. Antimicrob. Agents."},{"key":"7216_CR8","doi-asserted-by":"publisher","first-page":"1377","DOI":"10.1002\/med.21879","volume":"42","author":"Y Zhu","year":"2022","unstructured":"Zhu, Y. et al. Antimicrobial peptides, conventional antibiotics, and their synergistic utility for the treatment of drug\u2010resistant infections. Med. Res. Rev. 42, 1377\u20131422 (2022).","journal-title":"Med. Res. Rev."},{"key":"7216_CR9","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1038\/415389a","volume":"415","author":"M Zasloff","year":"2002","unstructured":"Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature 415, 389\u2013395 (2002).","journal-title":"Nature"},{"key":"7216_CR10","doi-asserted-by":"publisher","first-page":"926","DOI":"10.1038\/s42003-022-03899-4","volume":"5","author":"J Shi","year":"2022","unstructured":"Shi, J., Chen, C., Wang, D., Wang, Z. & Liu, Y. The antimicrobial peptide LI14 combats multidrug-resistant bacterial infections. Commun. Biol. 5, 926 (2022).","journal-title":"Commun. Biol."},{"key":"7216_CR11","doi-asserted-by":"publisher","first-page":"eaan4044","DOI":"10.1126\/scitranslmed.aan4044","volume":"10","author":"A de Breij","year":"2018","unstructured":"de Breij, A. et al. The antimicrobial peptide SAAP-148 combats drug-resistant bacteria and biofilms. Sci. Transl. Med. 10, eaan4044 (2018).","journal-title":"Sci. Transl. Med."},{"key":"7216_CR12","doi-asserted-by":"publisher","first-page":"975","DOI":"10.1038\/nature04051","volume":"437","author":"PH Mygind","year":"2005","unstructured":"Mygind, P. H. et al. Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus. Nature 437, 975\u2013980 (2005).","journal-title":"Nature"},{"key":"7216_CR13","doi-asserted-by":"publisher","first-page":"1168","DOI":"10.1126\/science.1185723","volume":"328","author":"T Schneider","year":"2010","unstructured":"Schneider, T., Kruse, T., Wimmer, R., Wiedemann, I. & Kristensen, H. H. Plectasin, a fungal defensin, targets the bacterial cell wall precursor lipid II. Science 328, 1168\u20131172 (2010).","journal-title":"Science"},{"key":"7216_CR14","doi-asserted-by":"publisher","first-page":"7565","DOI":"10.2147\/IJN.S180040","volume":"15","author":"AC Groo","year":"2018","unstructured":"Groo, A. C., Matougui, N., Umerska, A. & Saulnier, P. Reverse micelle-lipid nanocapsules: a novel strategy for drug delivery of the plectasin derivate AP138 antimicrobial peptide. Int. J. Nanomed. 15, 7565\u20137574 (2018).","journal-title":"Int. J. Nanomed."},{"key":"7216_CR15","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1007\/s00253-023-12947-w","volume":"108","author":"K Zhang","year":"2024","unstructured":"Zhang, K. et al. Expression and characterization of the new antimicrobial peptide AP138L-arg26 anti Staphylococcus aureus. Appl. Microbiol. Biotechnol. 108, 111 (2024).","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"7216_CR16","doi-asserted-by":"publisher","first-page":"201918427","DOI":"10.1073\/pnas.1918427117","volume":"117","author":"CG Starr","year":"2020","unstructured":"Starr, C. G., Ghimire, J., Guha, S., Hoffmann, J. P. & Wimley, W. C. Synthetic molecular evolution of host cell-compatible, antimicrobial peptides effective against drug-resistant, biofilm-forming bacteria. Proc. Natl. Acad. Sci. USA. 117, 201918427 (2020).","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"7216_CR17","doi-asserted-by":"publisher","first-page":"143a","DOI":"10.1016\/j.bpj.2020.11.1060","volume":"120","author":"J Ghimire","year":"2021","unstructured":"Ghimire, J., Starr, C. G., Guha, S., Hoffmann, J. P. & Wimley, W. C. Synthetic molecular evolution to identify hemocompatible antimicrobial peptides effective against drug-resistant, biofilm-forming bacteria. Biophys. J. 120, 143a (2021).","journal-title":"Biophys. J."},{"key":"7216_CR18","doi-asserted-by":"publisher","first-page":"5435","DOI":"10.3390\/ijms22115435","volume":"22","author":"H Liu","year":"2021","unstructured":"Liu, H. et al. Design and pharmacodynamics of recombinant fungus defensin NZL with improved activity against Staphylococcus hyicus in vitro and in vivo. Int. J. Mol. Sci. 22, 5435 (2021).","journal-title":"Int. J. Mol. Sci."},{"key":"7216_CR19","doi-asserted-by":"publisher","first-page":"681","DOI":"10.1007\/s00253-013-4881-2","volume":"98","author":"Y Zhang","year":"2014","unstructured":"Zhang, Y. et al. High expression of a plectasin-derived peptide NZ2114 in Pichia pastoris and its pharmacodynamics, postantibiotic and synergy against Staphylococcus aureus. Appl. Microbiol. Biotechnol. 98, 681\u2013694 (2014).","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"7216_CR20","doi-asserted-by":"publisher","first-page":"3492","DOI":"10.1074\/jbc.M117.805499","volume":"293","author":"D Nagarajan","year":"2018","unstructured":"Nagarajan, D., Tushar, R., Kulkarni, O., Ravichandran, S. & Mishra, M. Computational antimicrobial peptide design and evaluation against multidrug-resistant clinical isolates of bacteria. J.Bio. Chem. 293, 3492\u20133509 (2018).","journal-title":"J.Bio. Chem."},{"key":"7216_CR21","doi-asserted-by":"publisher","first-page":"bbab083","DOI":"10.1093\/bib\/bbab083","volume":"22","author":"J Xu","year":"2021","unstructured":"Xu, J., Li, F., Leier, A., Xiang, D. & Song, J. Comprehensive assessment of machine learning-based methods for predicting antimicrobial peptides. Brief. Bioinform. 22, bbab083 (2021).","journal-title":"Brief. Bioinform."},{"key":"7216_CR22","doi-asserted-by":"publisher","first-page":"D1094","DOI":"10.1093\/nar\/gkv1051","volume":"44","author":"FH Waghu","year":"2016","unstructured":"Waghu, F. H., Barai, R. S., Barai, P. & Idicula-Thomas, S. CAMPR3: a database on sequences, structures and signatures of antimicrobial peptides. Nucleic. Acids. Res. 44, D1094\u2013D1097 (2016).","journal-title":"Nucleic. Acids. Res."},{"key":"7216_CR23","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1002\/pro.3714","volume":"29","author":"FH Waghu","year":"2020","unstructured":"Waghu, F. H. & Idicula-Thomas, S. Collection of antimicrobial peptides database and its derivatives: Applications and beyond. Protein Sci 29, 36\u201342 (2020).","journal-title":"Protein Sci"},{"key":"7216_CR24","first-page":"421","volume":"50","author":"KA Higgins","year":"2010","unstructured":"Higgins, K. A., Bicknell, W., Keah, H. H. & Hearn, M. T. W. Comparison of the solution conformations of a human immunodeficiency virus peptidomimetic and its retro-inverso isomer using 1H NMR spectroscopy. Chem. Biol. Drug Des. 50, 421\u2013435 (2010).","journal-title":"Chem. Biol. Drug Des."},{"key":"7216_CR25","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1080\/26415275.2020.1796674","volume":"7","author":"P Parvekar","year":"2020","unstructured":"Parvekar, P., Palaskar, J. N., Metgud, S., Maria, R. & Dutta, S. The minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) of silver nanoparticles against Staphylococcus aureus. Biomaterial Invest. Dentis. 7, 105\u2013109 (2020).","journal-title":"Biomaterial Invest. Dentis."},{"key":"7216_CR26","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1016\/j.biomaterials.2011.09.084","volume":"33","author":"H Tan","year":"2012","unstructured":"Tan, H. et al. The use of quaternised chitosan-loaded PMMA to inhibit biofilm formation and downregulate the virulence-associated gene expression of antibiotic-resistant staphylococcus. Biomaterials 33, 365\u2013377 (2012).","journal-title":"Biomaterials"},{"key":"7216_CR27","doi-asserted-by":"publisher","first-page":"7630","DOI":"10.1021\/acs.jmedchem.1c00334","volume":"66","author":"J Wang","year":"2021","unstructured":"Wang, J., Ansari, M. F. & Zhou, C. H. Identification of unique quinazolone thiazoles as novel structural scaffolds for potential gram-negative bacterial conquerors. J. Med. Chem. 66, 7630\u20137645 (2021).","journal-title":"J. Med. Chem."},{"key":"7216_CR28","doi-asserted-by":"publisher","first-page":"19446","DOI":"10.1073\/pnas.2005540117","volume":"117","author":"JL Narayana","year":"2020","unstructured":"Narayana, J. L. et al. Two distinct amphipathic peptide antibiotics with systemic efficacy. Proc. Natl. Acad. Sci. USA. 117, 19446\u201319454 (2020).","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"7216_CR29","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00018-021-04071-7","volume":"79","author":"PF She","year":"2022","unstructured":"She, P. F. et al. L007-0069 kills Staphylococcus aureus in high resistant phenotypes. Cell. Mol. Life Sci. 79, 1\u201316 (2022).","journal-title":"Cell. Mol. Life Sci."},{"key":"7216_CR30","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1093\/jac\/31.suppl_D.55","volume":"35","author":"N Frimodt-Moller","year":"1993","unstructured":"Frimodt-Moller, N. The mouse peritonitis model: present and future use. J. Antimicrob. Chemother. 35, 55\u201360 (1993).","journal-title":"J. Antimicrob. Chemother."},{"key":"7216_CR31","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1093\/humrep\/dey361","volume":"3434","author":"SW Yan","year":"2019","unstructured":"Yan, S. W. The establishment of a mouse model of deep endometriosis. Hum. Reprod. 3434, 235\u2013247 (2019).","journal-title":"Hum. Reprod."},{"key":"7216_CR32","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1186\/s13756-018-0423-0","volume":"7","author":"RC Founou","year":"2018","unstructured":"Founou, R. C., Founou, L. L. & Essack, S. Y. Extended spectrum beta-lactamase mediated resistance in carriage and clinical gram-negative ESKAPE bacteria: a comparative study between a district and tertiary hospital in South Africa. Antimicrob. Resist. Infect. Control 7, 134 (2018).","journal-title":"Antimicrob. Resist. Infect. Control"},{"key":"7216_CR33","doi-asserted-by":"publisher","first-page":"3319","DOI":"10.1111\/1541-4337.12757","volume":"20","author":"Z Huang","year":"2021","unstructured":"Huang, Z. et al. Phages and their lysins: toolkits in the battle against foodborne pathogens in the postantibiotic era. Compr. Rev. Food. Sci. Food Saf. 20, 3319\u20133343 (2021).","journal-title":"Compr. Rev. Food. Sci. Food Saf."},{"key":"7216_CR34","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1128\/microbiolspec.ARBA-0009-2017","volume":"6","author":"SA Mcewen","year":"2018","unstructured":"Mcewen, S. A. & Collignon, P. J. Antimicrobial resistance: a one health perspective. Microbiol. Spectrum. 6, 10 (2018).","journal-title":"Microbiol. Spectrum."},{"key":"7216_CR35","doi-asserted-by":"publisher","first-page":"607","DOI":"10.1007\/s40259-023-00608-3","volume":"37","author":"CS Bernardo","year":"2023","unstructured":"Bernardo, C. S. et al. Going beyond host defence peptides: horizons of chemically engineered peptides for multidrug-resistant bacteria. BioDrugs 37, 607\u2013623 (2023).","journal-title":"BioDrugs"},{"key":"7216_CR36","doi-asserted-by":"publisher","DOI":"10.1002\/pep2.24122","volume":"111","author":"HB Koo","year":"2019","unstructured":"Koo, H. B. & Seo, J. Antimicrobial peptides under clinical investigation. Pept. Sci. 111, e24122 (2019).","journal-title":"Pept. Sci."},{"key":"7216_CR37","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1094\/MPMI-8-0006","volume":"8","author":"RA Gururaj","year":"1995","unstructured":"Gururaj, R. A. Antimicrobial peptides. MPMI 8, 6\u201313 (1995).","journal-title":"MPMI"},{"key":"7216_CR38","doi-asserted-by":"publisher","DOI":"10.1002\/smll.201701316","volume":"13","author":"M Pillong","year":"2017","unstructured":"Pillong, M. et al. Peptides: rational design of membrane\u2010pore\u2010forming peptides. Small 13, 1701316 (2017).","journal-title":"Small"},{"key":"7216_CR39","doi-asserted-by":"publisher","first-page":"12316","DOI":"10.1074\/jbc.M413406200","volume":"280","author":"YX Chen","year":"2005","unstructured":"Chen, Y. X. et al. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity\/therapeutic index. J. Biolog. Chem. 280, 12316\u201312329 (2005).","journal-title":"J. Biolog. Chem."},{"key":"7216_CR40","doi-asserted-by":"publisher","first-page":"3134","DOI":"10.3390\/ijms24043134","volume":"24","author":"K Zhang","year":"2023","unstructured":"Zhang, K. et al. Thinking on the construction of antimicrobial peptide databases: powerful tools for the molecular design and screening. Int. J. Mol. Sci. 24, 3134 (2023).","journal-title":"Int. J. Mol. Sci."},{"key":"7216_CR41","doi-asserted-by":"publisher","first-page":"9221","DOI":"10.1039\/D1SC01713F","volume":"12","author":"A Capecchi","year":"2021","unstructured":"Capecchi, A. et al. Machine learning designs non-hemolytic antimicrobial peptides. Chem. Sci. 12, 9221\u20139232 (2021).","journal-title":"Chem. Sci."},{"key":"7216_CR42","doi-asserted-by":"publisher","first-page":"9161","DOI":"10.1021\/bi1011578","volume":"49","author":"S Leptihn","year":"2010","unstructured":"Leptihn, S. Correlation of charge, hydrophobicity, and structure with antimicrobial activity of S1 and MIRIAM peptides. Biochemistry 49, 9161\u20139170 (2010).","journal-title":"Biochemistry"},{"key":"7216_CR43","doi-asserted-by":"publisher","first-page":"107962","DOI":"10.1016\/j.biotechadv.2022.107962","volume":"59","author":"Z Lai","year":"2022","unstructured":"Lai, Z. et al. Strategies employed in the design of antimicrobial peptides with enhanced proteolytic stability. Biotechnol. Adv. 59, 107962 (2022).","journal-title":"Biotechnol. Adv."},{"key":"7216_CR44","doi-asserted-by":"publisher","first-page":"256","DOI":"10.1002\/ptr.6823","volume":"35","author":"S Srivastava","year":"2021","unstructured":"Srivastava, S. et al. Cysteine-rich antimicrobial peptides from plants: the future of antimicrobial therapy. Phytother. Res. 35, 256\u2013277 (2021).","journal-title":"Phytother. Res."},{"key":"7216_CR45","doi-asserted-by":"publisher","first-page":"7468","DOI":"10.1021\/acs.joc.0c00871","volume":"85","author":"TA Dietsche","year":"2021","unstructured":"Dietsche, T. A., Eldesouky, H. E., Zeiders, S. M., Seleem, M. N. & Chmielewski, J. Targeting intracellular pathogenic bacteria through N-terminal modification of cationic amphiphilic polyproline helices. J. Org. Chem. 85, 7468\u20137475 (2021).","journal-title":"J. Org. Chem."},{"key":"7216_CR46","doi-asserted-by":"publisher","first-page":"5301","DOI":"10.1007\/s00253-014-5732-5","volume":"98","author":"M Ahmad","year":"2014","unstructured":"Ahmad, M., Hirz, M., Pichler, H. & Schwab, H. Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production. Appl. Microbiol. Biotechnol. 98, 5301\u20135317 (2014).","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"7216_CR47","doi-asserted-by":"publisher","first-page":"905","DOI":"10.1038\/nbt0893-905","volume":"11","author":"JM Cregg","year":"1993","unstructured":"Cregg, J. M., Vedvick, T. S. & Raschke, W. C. Recent advances in the expression of foreign genes in Pichia pastoris. Nat. Biotechnol. 11, 905\u2013910 (1993).","journal-title":"Nat. Biotechnol."},{"key":"7216_CR48","doi-asserted-by":"publisher","first-page":"100","DOI":"10.1111\/j.1467-7652.2010.00538.x","volume":"9","author":"SB Lee","year":"2010","unstructured":"Lee, S. B., Li, B., Jin, S. & Daniell, H. Expression and characterization of antimicrobial peptides Retrocyclin-101 and Protegrin-1 in chloroplasts to control viral and bacterial infections. Plant Biotechnol. J. 9, 100\u2013115 (2010).","journal-title":"Plant Biotechnol. J."},{"key":"7216_CR49","doi-asserted-by":"publisher","first-page":"189","DOI":"10.1016\/j.pep.2011.04.014","volume":"78","author":"J Zhang","year":"2011","unstructured":"Zhang, J. et al. Expression of plectasin in Pichia pastoris and its characterization as a new antimicrobial peptide against Staphyloccocus and Streptococcus. Protein Expres. Purif. 78, 189\u2013196 (2011).","journal-title":"Protein Expres. Purif."},{"key":"7216_CR50","doi-asserted-by":"publisher","first-page":"eaau5480","DOI":"10.1126\/science.aau5480","volume":"368","author":"BP Lazzaro","year":"2020","unstructured":"Lazzaro, B. P., Zasloff, M. & Rolff, J. Antimicrobial peptides: application informed by evolution. Science 368, eaau5480 (2020).","journal-title":"Science"},{"key":"7216_CR51","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1007\/978-981-13-3588-4_1","volume":"1117","author":"M Zasloff","year":"2019","unstructured":"Zasloff, M. Antimicrobial peptides of multicellular organisms: my perspective. Adv. Exp. Med. Biol. 1117, 3\u20136 (2019).","journal-title":"Adv. Exp. Med. Biol."},{"key":"7216_CR52","doi-asserted-by":"publisher","first-page":"2649","DOI":"10.1007\/s00253-014-6077-9","volume":"99","author":"X Cao","year":"2015","unstructured":"Cao, X. et al. Design and recombination expression of a novel plectasin-derived peptide MP1106 and its properties against Staphylococcus aureus. Appl. Microbiol. Biotechnol. 99, 2649\u20132662 (2015).","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"7216_CR53","doi-asserted-by":"publisher","first-page":"1057","DOI":"10.3389\/fmicb.2020.01057","volume":"11","author":"B Li","year":"2020","unstructured":"Li, B. et al. An enhanced variant designed from DLP4 cationic peptide against Staphylococcus aureus CVCC 546. Front. Microbiol. 11, 1057 (2020).","journal-title":"Front. Microbiol."},{"key":"7216_CR54","first-page":"445","volume":"2","author":"NK Archer","year":"2011","unstructured":"Archer, N. K., Mazaitis, M. J., Costerton, J. W., Leid, J. G. & Shirtliff, M. E. Staphylococcus aureus biofilms. Laryngoscope 2, 445\u2013459 (2011).","journal-title":"Laryngoscope"},{"key":"7216_CR55","first-page":"1499","volume":"13","author":"P Speziale","year":"2008","unstructured":"Speziale, P., Visai, L., Rindi, S., Pietrocola, G. & Provenza, G. Prevention and treatment of staphylococcus biofilms. Curr. Med. Chem. 13, 1499\u20131516 (2008).","journal-title":"Curr. Med. Chem."},{"key":"7216_CR56","doi-asserted-by":"publisher","first-page":"1750","DOI":"10.1016\/j.jiph.2021.10.020","volume":"14","author":"TM Uddin","year":"2021","unstructured":"Uddin, T. M. et al. Antibiotic resistance in microbes: history, mechanisms, therapeutic strategies and future prospects. J. Infect. Public Health 14, 1750\u20131766 (2021).","journal-title":"J. Infect. Public Health"},{"key":"7216_CR57","doi-asserted-by":"publisher","first-page":"8437","DOI":"10.1073\/pnas.1918427117","volume":"117","author":"CG Starr","year":"2020","unstructured":"Starr, C. G. et al. Synthetic molecular evolution of host cell-compatible, antimicrobial peptides effective against drug-resistant, biofilm-forming bacteria. Proc. Natl. Acad. Sci. USA. 117, 8437\u20138448 (2020).","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"7216_CR58","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1016\/S0966-842X(00)01913-2","volume":"9","author":"TF Mah","year":"2001","unstructured":"Mah, T. F. & O\u2019Toole, G. A. Mechanisms of biofilm resistance to antimicrobial agents. Trends Microbiol 9, 34\u201339 (2001).","journal-title":"Trends Microbiol"},{"key":"7216_CR59","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1038\/s42003-020-0761-3","volume":"3","author":"Z Wang","year":"2020","unstructured":"Wang, Z. et al. Development of chimeric peptides to facilitate the neutralisation of lipopolysaccharides during bactericidal targeting of multidrug-resistant. Commun. Biol. 3, 41 (2020).","journal-title":"Commun. Biol."},{"key":"7216_CR60","volume":"120","author":"A Ariasrojas","year":"2023","unstructured":"Ariasrojas, A., Frahm, D., Hurwitz, R., Brinkmann, V. & Iatsenko, I. Resistance to host antimicrobial peptides mediates resilience of gut commensals during infection and aging in Drosophila. bioRxiv 120, e2305649120 (2023).","journal-title":"bioRxiv"},{"key":"7216_CR61","doi-asserted-by":"publisher","first-page":"1181","DOI":"10.1016\/j.ajic.2019.04.001","volume":"47","author":"AT Khler","year":"2019","unstructured":"Khler, A. T., Rodloff, A. C., Labahn, M., Reinhardt, M. & Speck, S. Evaluation of disinfectant efficacy against multidrug-resistant bacteria: a comprehensive analysis of different methods. Am. J. Infect. Control 47, 1181\u20131187 (2019).","journal-title":"Am. J. Infect. Control"},{"key":"7216_CR62","doi-asserted-by":"publisher","first-page":"1443","DOI":"10.1016\/j.fertnstert.2021.03.023","volume":"115","author":"K Kitaya","year":"2021","unstructured":"Kitaya, K. & Ishikawa, T. Chronic endometritis: simple can be harder than complex? Fertil. Steril. 115, 1443\u20131444 (2021).","journal-title":"Fertil. Steril."},{"key":"7216_CR63","doi-asserted-by":"publisher","DOI":"10.1186\/s12958-018-0414-2","volume":"16","author":"A Bashiri","year":"2018","unstructured":"Bashiri, A., Halper, K. I. & Orvieto, R. Recurrent implantation failure-update overview on etiology, diagnosis, treatment and future directions. Reprod. Biol. Endocrinol. 16, 121 (2018).","journal-title":"Reprod. Biol. Endocrinol."},{"key":"7216_CR64","doi-asserted-by":"publisher","first-page":"1445","DOI":"10.1016\/j.fertnstert.2021.03.025","volume":"115","author":"E Cicinelli","year":"2021","unstructured":"Cicinelli, E., Cicinelli, R. & Vitagliano, A. Antibiotic therapy for chronic endometritis and its reproductive implications: a step forward, with some uncertainties. Fertil. Steril. 115, 1445\u20131446 (2021).","journal-title":"Fertil. Steril."},{"key":"7216_CR65","doi-asserted-by":"publisher","first-page":"888540","DOI":"10.3389\/fmicb.2022.888540","volume":"13","author":"Y Hao","year":"2022","unstructured":"Hao, Y., Wang, J., de la Fuente-Nunez, C. & Franco, O. L. Editorial: antimicrobial peptides: molecular design, structure-function relationship, and biosynthesis optimization. Front. Microbiol. 13, 888540 (2022).","journal-title":"Front. Microbiol."},{"key":"7216_CR66","doi-asserted-by":"publisher","first-page":"1125426","DOI":"10.3389\/fmicb.2023.1125426","volume":"14","author":"N Yang","year":"2023","unstructured":"Yang, N., Aminov, R., Franco, O. L., de la Fuente-Nunez, C. & Wang, J. Editorial: community series in antimicrobial peptides: molecular design, structure function relationship and biosynthesis optimization. Front. Microbiol. 14, 1125426 (2023).","journal-title":"Front. Microbiol."},{"key":"7216_CR67","doi-asserted-by":"publisher","first-page":"1425952","DOI":"10.3389\/fmicb.2024.1425952","volume":"15","author":"X Ma","year":"2024","unstructured":"Ma, X. et al. Editorial: Antimicrobial peptides and their druggability, bio-safety, stability, and resistance. Front. Microbiol. 15, 1425952 (2024).","journal-title":"Front. Microbiol."},{"key":"7216_CR68","doi-asserted-by":"publisher","first-page":"1956","DOI":"10.1128\/AAC.01901-13","volume":"58","author":"LG Monahan","year":"2014","unstructured":"Monahan, L. G. et al. Rapid conversion of Pseudomonas aeruginosa to a spherical cell morphotype facilitates tolerance to carbapenems and penicillins but increases susceptibility to antimicrobial peptides. Antimicrob. Agents. Chemother. 58, 1956\u20131962 (2014).","journal-title":"Antimicrob. Agents. Chemother."},{"key":"7216_CR69","doi-asserted-by":"publisher","first-page":"D288","DOI":"10.1093\/nar\/gkaa991","volume":"49","author":"P Malak","year":"2021","unstructured":"Malak, P. et al. DBAASP v3: database of antimicrobial\/cytotoxic activity and structure of peptides as a resource for development of new therapeutics. Nucleic. Acids. Res. 49, D288\u2013D297 (2021).","journal-title":"Nucleic. Acids. Res."},{"key":"7216_CR70","doi-asserted-by":"publisher","first-page":"D1087","DOI":"10.1093\/nar\/gkv1278","volume":"44","author":"G Wang","year":"2016","unstructured":"Wang, G., Li, X. & Wang, Z. APD3: the antimicrobial peptide database as a tool for research and education. Nucleic. Acids. Res. 44, D1087\u2013D1093 (2016).","journal-title":"Nucleic. Acids. Res."},{"key":"7216_CR71","doi-asserted-by":"publisher","first-page":"W174","DOI":"10.1093\/nar\/gkv342","volume":"43","author":"J Yang","year":"2015","unstructured":"Yang, J. & Zhang, Y. I-TASSER server: new development for protein structure and function predictions. Nucleic. Acids. Res. 43, W174\u2013W181 (2015).","journal-title":"Nucleic. Acids. Res."},{"key":"7216_CR72","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1038\/nprot.2007.521","volume":"3","author":"I Wiegand","year":"2008","unstructured":"Wiegand, I., Kai, H. & Hancock, R. Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances. Nat. Protoc. 3, 163\u2013175 (2008).","journal-title":"Nat. Protoc."},{"key":"7216_CR73","doi-asserted-by":"publisher","first-page":"865774","DOI":"10.3389\/fmicb.2022.865774","volume":"13","author":"X Zheng","year":"2022","unstructured":"Zheng, X. et al. Pharmacokinetics and pharmacodynamics of fungal defensin NZX against Staphylococcus aureus-induced mouse peritonitis model. Front. Microbiol. 13, 865774 (2022).","journal-title":"Front. Microbiol."},{"key":"7216_CR74","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.jconrel.2015.12.003","volume":"222","author":"A de Breij","year":"2016","unstructured":"de Breij, A. et al. Prevention of Staphylococcus aureus biomaterial-associated infections using a polymer-lipid coating containing the antimicrobial peptide OP-145. J. Control Release 222, 1\u20138 (2016).","journal-title":"J. Control Release"},{"key":"7216_CR75","doi-asserted-by":"publisher","first-page":"5973","DOI":"10.3390\/ijms21175973","volume":"21","author":"I Nagaoka","year":"2020","unstructured":"Nagaoka, I., Tamura, H. & Reich, J. Therapeutic potential of cathelicidin peptide LL-37, an antimicrobial agent, in a murine sepsis model. Int. J. Mol. Sci 21, 5973 (2020).","journal-title":"Int. J. Mol. Sci"},{"key":"7216_CR76","doi-asserted-by":"publisher","first-page":"106508","DOI":"10.1016\/j.domaniend.2020.106508","volume":"74","author":"Y Miao","year":"2020","unstructured":"Miao, Y., Ishfaq, M., Liu, Y., Wu, Z. & Li, J. Baicalin attenuates endometritis in a rabbit model induced by infection with Escherichia coli and Staphylococcus aureus via NF-\u03baB and JNK signaling pathways. Domest. Anim. Endocrinol. 74, 106508 (2020).","journal-title":"Domest. Anim. Endocrinol."}],"container-title":["Communications Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s42003-024-07216-z.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s42003-024-07216-z","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s42003-024-07216-z.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,11,27]],"date-time":"2024-11-27T13:02:53Z","timestamp":1732712573000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s42003-024-07216-z"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,11,27]]},"references-count":76,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2024,12]]}},"alternative-id":["7216"],"URL":"https:\/\/doi.org\/10.1038\/s42003-024-07216-z","relation":{},"ISSN":["2399-3642"],"issn-type":[{"value":"2399-3642","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,11,27]]},"assertion":[{"value":"24 June 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 November 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 November 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}},{"value":"The mouse experiment was performed according to the Animal Care and Use Committee of the Feed Research Institute of the Chinese Academy of Agricultural Sciences (CAAS) and approved by the Laboratory Animal Ethical Committee and its Inspection of the Feed Research Institute of CAAS (IFR-CAAS-20230818).","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical approval"}}],"article-number":"1582"}}