{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T21:37:34Z","timestamp":1791841054655,"version":"4.3.4"},"reference-count":146,"publisher":"MDPI AG","issue":"23","license":[{"start":{"date-parts":[[2019,11,22]],"date-time":"2019-11-22T00:00:00Z","timestamp":1574380800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100007479","name":"Fondazione Cassa di Risparmio di Padova e Rovigo","doi-asserted-by":"publisher","award":["Progetti di Eccellenza 2011\/12"],"award-info":[{"award-number":["Progetti di Eccellenza 2011\/12"]}],"id":[{"id":"10.13039\/100007479","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003500","name":"Universit\u00e0 degli Studi di Padova","doi-asserted-by":"publisher","award":["CPDA154301"],"award-info":[{"award-number":["CPDA154301"]}],"id":[{"id":"10.13039\/501100003500","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010665","name":"H2020 Marie Sk\u0142odowska-Curie Actions","doi-asserted-by":"publisher","award":["Cinchron (grant agreement 765937)"],"award-info":[{"award-number":["Cinchron (grant agreement 765937)"]}],"id":[{"id":"10.13039\/100010665","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The alarming escalation of infectious diseases resistant to conventional antibiotics requires urgent global actions, including the development of new therapeutics. Antimicrobial peptides (AMPs) represent potential alternatives in the treatment of multi-drug resistant (MDR) infections. Here, we focus on Cecropins (Cecs), a group of naturally occurring AMPs in insects, and on synthetic Cec-analogs. We describe their action mechanisms and antimicrobial activity against MDR bacteria and other pathogens. We report several data suggesting that Cec and Cec-analog peptides are promising antibacterial therapeutic candidates, including their low toxicity against mammalian cells, and anti-inflammatory activity. We highlight limitations linked to the use of peptides as therapeutics and discuss methods overcoming these constraints, particularly regarding the introduction of nanotechnologies. New formulations based on natural Cecs would allow the development of drugs active against Gram-negative bacteria, and those based on Cec-analogs would give rise to therapeutics effective against both Gram-positive and Gram-negative pathogens. Cecs and Cec-analogs might be also employed to coat biomaterials for medical devices as an approach to prevent biomaterial-associated infections. The cost of large-scale production is discussed in comparison with the economic and social burden resulting from the progressive diffusion of MDR infectious diseases.<\/jats:p>","DOI":"10.3390\/ijms20235862","type":"journal-article","created":{"date-parts":[[2019,11,22]],"date-time":"2019-11-22T09:02:52Z","timestamp":1574413372000},"page":"5862","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":179,"title":["Insect Cecropins, Antimicrobial Peptides with Potential Therapeutic Applications"],"prefix":"10.3390","volume":"20","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9086-917X","authenticated-orcid":false,"given":"Daniel","family":"Brady","sequence":"first","affiliation":[{"name":"Department of Biology, University of Padova, via U. Bassi 58\/B, 35131 Padova, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9255-4294","authenticated-orcid":false,"given":"Alessandro","family":"Grapputo","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Padova, via U. Bassi 58\/B, 35131 Padova, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7608-2650","authenticated-orcid":false,"given":"Ottavia","family":"Romoli","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Padova, via U. Bassi 58\/B, 35131 Padova, Italy"},{"name":"Institut Pasteur de la Guyane, 23 Avenue Pasteur, 97306 Cayenne, French Guiana, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5631-7467","authenticated-orcid":false,"given":"Federica","family":"Sandrelli","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Padova, via U. Bassi 58\/B, 35131 Padova, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,11,22]]},"reference":[{"key":"ref_1","unstructured":"(2019). Report to the Secretary General of the Nations: No Time to Wait\u2013Securing the Future from Drug-Resistant Infections, Interagency Coordination Group on Antimicrobial Resistance (IACG)."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"R14-9","DOI":"10.1016\/j.cub.2015.11.017","article-title":"Antimicrobial peptides","volume":"26","author":"Zhang","year":"2016","journal-title":"Curr. Biol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Kumar, P., Kizhakkedathu, J.N., and Straus, S.K. (2018). Antimicrobial peptides: Diversity, mechanism of action and strategies to improve the activity and biocompatibility in vivo. Biomolecules, 8.","DOI":"10.3390\/biom8010004"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"D1087","DOI":"10.1093\/nar\/gkv1278","article-title":"APD3: The antimicrobial peptide database as a tool for research and education","volume":"44","author":"Wang","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Wu, Q., Pato\u010dka, J., and Ku\u010da, K. (2018). Insect antimicrobial peptides, a mini review. Toxins, 10.","DOI":"10.3390\/toxins10110461"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"554","DOI":"10.2174\/1568026616666160713123654","article-title":"The medical potential of antimicrobial peptides from insects","volume":"17","author":"Tonk","year":"2017","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"5807","DOI":"10.1007\/s00253-014-5792-6","article-title":"Insect antimicrobial peptides and their applications","volume":"98","author":"Yi","year":"2014","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1111\/j.1432-1033.1980.tb05991.x","article-title":"Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia","volume":"106","author":"Hultmark","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1111\/j.1432-1033.1982.tb06857.x","article-title":"Insect immunity: Isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae","volume":"127","author":"Hultmark","year":"1982","journal-title":"Eur. J. Biochem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1038\/292246a0","article-title":"Sequence and specificity of two antibacterial proteins involved in insect immunity","volume":"292","author":"Steiner","year":"1981","journal-title":"Nature"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"20150290","DOI":"10.1098\/rstb.2015.0290","article-title":"Diversity, evolution and medical applications of insect antimicrobial peptides","volume":"371","author":"Mylonakis","year":"2016","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1126\/science.1257570","article-title":"Phylogenomics resolves the timing and pattern of insect evolution","volume":"346","author":"Misof","year":"2014","journal-title":"Science"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/S0014-5793(97)00769-2","article-title":"cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate, Styela clava","volume":"412","author":"Zhao","year":"1997","journal-title":"FEBS Lett."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"9159","DOI":"10.1073\/pnas.86.23.9159","article-title":"Antibacterial peptides from pig intestine: Isolation of a mammalian cecropin","volume":"86","author":"Lee","year":"1989","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1007\/s000180300051","article-title":"Ascaris nematodes from pig and human make three anti-bacterial peptides: Isolation of cecropin P1 and two ASABF peptides","volume":"60","author":"Andersson","year":"2003","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S0014-5793(99)00582-7","article-title":"The origin of cecropins; implications from synthetic peptides derived from ribosomal protein L1","volume":"451","author":"Normark","year":"1999","journal-title":"FEBS Lett."},{"key":"ref_17","first-page":"94","article-title":"The cecropin superfamily of toxic peptides","volume":"11","author":"Tamang","year":"2006","journal-title":"J. Mol. Microbiol. Biotechnol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/j.dci.2011.09.007","article-title":"Distribution and characteristics of ABFs, cecropins, nemapores, and lysozymes in nematodes","volume":"36","author":"Tarr","year":"2012","journal-title":"Dev. Comp. Immunol."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Segovia, L.J.T., Ramirez, G.A.T., Arias, D.C.H., Duran, J.D.R., Bedoya, J.P., and Osorio, J.C.C. (2017). Identification and characterization of novel cecropins from the Oxysternon conspicillatum neotropic dung beetle. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0187914"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/j.cbpb.2005.08.001","article-title":"Purification and cDNA cloning of a cecropin from the longicorn beetle, Acalolepta luxuriosa","volume":"142","author":"Saito","year":"2005","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1007\/s10989-012-9320-1","article-title":"A novel antimicrobial peptide derived from the insect Paederus dermatitis","volume":"19","author":"Asoodeh","year":"2013","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1186\/s13071-015-1176-8","article-title":"A cecropin-like antimicrobial peptide with anti-inflammatory activity from the black fly salivary glands","volume":"8","author":"Wu","year":"2015","journal-title":"Parasites Vectors"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1046\/j.1365-2583.2000.00164.x","article-title":"Cloning and analysis of a cecropin gene from the malaria vector mosquito, Anopheles gambiae","volume":"9","author":"Vizioli","year":"2000","journal-title":"Insect Mol. Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"20092","DOI":"10.1074\/jbc.274.29.20092","article-title":"Antimicrobial activity spectrum, cDNA cloning, and mRNA expression of a newly isolated member of the cecropin family from the mosquito vector Aedes aegypti","volume":"274","author":"Lowenberger","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1728","DOI":"10.1128\/AAC.04198-14","article-title":"Insect-derived cecropins display activity against Acinetobacter baumannii in a whole-animal high-throughput Caenorhabditis elegans model","volume":"59","author":"Jayamani","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1186\/s13071-018-3000-8","article-title":"Anti-inflammatory activities of Aedes aegypti cecropins and their protection against murine endotoxin shock","volume":"11","author":"Wei","year":"2018","journal-title":"Parasites Vectors"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1006\/bbrc.1998.9150","article-title":"Peptide sequence of an antibiotic cecropin from the vector mosquito, Aedes albopictus","volume":"249","author":"Sun","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.dci.2016.05.018","article-title":"Antimicrobial activity of mosquito cecropin peptides against Francisella","volume":"63","author":"Kaushal","year":"2016","journal-title":"Dev. Comp. Immunol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1074\/mcp.M700497-MCP200","article-title":"Toward an understanding of the molecular mechanism for successful blood feeding by coupling proteomics analysis with pharmacological testing of horsefly salivary glands","volume":"7","author":"Xu","year":"2008","journal-title":"Mol. Cell. Proteomics"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1111\/1748-5967.12226","article-title":"A novel cecropin-like peptide from black soldier fly, Hermetia illucens: Isolation, structural and functional characterization","volume":"47","author":"Park","year":"2017","journal-title":"Entomol. Res."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1016\/S0965-1748(99)00071-5","article-title":"Drosophila cecropin as an antifungal agent","volume":"29","author":"Ekengren","year":"1999","journal-title":"Insect Biochem. Mol. Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2969","DOI":"10.1002\/j.1460-2075.1990.tb07489.x","article-title":"The immune response in Drosophila: Pattern of cecropin expression and biological activity","volume":"9","author":"Samakovlis","year":"1990","journal-title":"EMBO J."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1007\/s00253-011-3793-2","article-title":"Bactericidal activity of Musca domestica cecropin (Mdc) on multidrug-resistant clinical isolate of Escherichia coli","volume":"95","author":"Lu","year":"2012","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2169","DOI":"10.1007\/s00253-010-2606-3","article-title":"Expression of the antimicrobial peptide cecropin fused with human lysozyme in Escherichia coli","volume":"87","author":"Lu","year":"2010","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"657536","DOI":"10.1155\/2014\/657536","article-title":"Transmission electron microscopic morphological study and flow cytometric viability assessment of Acinetobacter baumannii susceptible to Musca domestica cecropin","volume":"2014","author":"Gui","year":"2014","journal-title":"Sci. World J."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/S0965-1748(02)00029-2","article-title":"Immunopeptides in the defense reactions of Glossina morsitans to bacterial and Trypanosoma brucei brucei infections","volume":"32","author":"Boulanger","year":"2002","journal-title":"Insect Biochem. Mol. Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"49921","DOI":"10.1074\/jbc.M206296200","article-title":"Epithelial innate immunity. A novel antimicrobial peptide with antiparasitic activity in the blood-sucking insect Stomoxys calcitrans","volume":"277","author":"Boulanger","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1042\/bj2110727","article-title":"Purification and characterization of an antibacterial protein from haemolymph of Sarcophaga peregrina (flesh-fly) larvae","volume":"211","author":"Okada","year":"1983","journal-title":"Biochem. J."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1042\/bj2220119","article-title":"Mode of action of a bactericidal protein induced in the haemolymph of Sarcophaga peregrina (flesh-fly) larvae","volume":"222","author":"Okada","year":"1984","journal-title":"Biochem. J."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"7174","DOI":"10.1016\/S0021-9258(17)39590-X","article-title":"Primary structure of sarcotoxin I, an antibacterial protein induced in the hemolymph of Sarcophaga peregrina (flesh fly) larvae","volume":"260","author":"Okada","year":"1985","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2508","DOI":"10.1128\/AAC.05180-14","article-title":"Antimicrobial peptides expressed in medicinal maggots of the blow fly Lucilia sericata show combinatorial activity against bacteria","volume":"59","author":"Vogel","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1046\/j.1365-280X.1998.00160.x","article-title":"Fungicidal and binding properties of the natural peptides cecropin B and dermaseptin","volume":"36","author":"Bland","year":"1998","journal-title":"Med. Mycol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1099\/0022-1317-79-4-731","article-title":"Antimicrobial peptides melittin and cecropin inhibit replication of human immunodeficiency virus 1 by suppressing viral gene expression","volume":"79","author":"Wachinger","year":"1998","journal-title":"J. Gen. Virol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1007\/s430-001-8025-x","article-title":"Cecropins, antibacterial peptides from insects and mammals, are potently fungicidal against Candida albicans","volume":"189","author":"Berninghausen","year":"2001","journal-title":"Med. Microbiol. Immunol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1002\/arch.21193","article-title":"Anti-inflammatory activities of cecropin a and its mechanism of action","volume":"88","author":"Lee","year":"2015","journal-title":"Arch. Insect Biochem. Physiol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.1093\/jac\/37.6.1077","article-title":"Antimicrobial activity of cecropins","volume":"37","author":"Moore","year":"1996","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.meegid.2015.06.021","article-title":"Inhibition of porcine reproductive and respiratory syndrome virus by Cecropin D in vitro","volume":"34","author":"Liu","year":"2015","journal-title":"Infect. Genet. Evol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1111\/j.1432-1033.1982.tb06858.x","article-title":"Insect immunity: Isolation and structure of cecropins B and D from pupae of the Chinese oak silk moth, Antheraea pernyi","volume":"127","author":"Qu","year":"1982","journal-title":"Eur. J. Biochem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"e5369","DOI":"10.7717\/peerj.5369","article-title":"A novel cecropin B-derived peptide with antibacterial and potential anti-inflammatory properties","volume":"6","author":"Wang","year":"2018","journal-title":"PeerJ"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"e21368","DOI":"10.1002\/arch.21368","article-title":"Characterization and functional study of a Cecropin-like peptide from the Chinese oak silkworm, Antheraea pernyi","volume":"94","author":"Fang","year":"2017","journal-title":"Arch. Insect Biochem. Physiol."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Yang, W., Cheng, T., Ye, M., Deng, X., Yi, H., Huang, Y., Tan, X., Han, D., Wang, B., and Xiang, Z. (2011). Functional divergence among silkworm antimicrobial peptide paralogs by the activities of recombinant proteins and the induced expression profiles. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0018109"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.gene.2016.02.045","article-title":"Bombyx mori cecropin A has a high antifungal activity to entomopathogenic fungus Beauveria bassiana","volume":"583","author":"Lu","year":"2016","journal-title":"Gene"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1021\/acsinfecdis.9b00042","article-title":"Enhanced Silkworm Cecropin B Antimicrobial Activity against Pseudomonas aeruginosa from Single Amino Acid Variation","volume":"5","author":"Romoli","year":"2019","journal-title":"ACS Infect. Dis."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"4237","DOI":"10.1128\/AEM.02435-10","article-title":"Anti-Listeria activities of Galleria mellonella hemolymph proteins","volume":"77","author":"Mukherjee","year":"2011","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/ja.2016.134","article-title":"Antimicrobial activity and interactions of cationic peptides derived from Galleria mellonella cecropin D-like peptide with model membranes","volume":"70","author":"Trier","year":"2017","journal-title":"J. Antibiot. (Tokyo)"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1007\/s10059-010-0050-y","article-title":"Characterization and cDNA cloning of a cecropin-like antimicrobial peptide, papiliocin, from the swallowtail butterfly, Papilio xuthus","volume":"29","author":"Kim","year":"2010","journal-title":"Mol. Cells"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"41296","DOI":"10.1074\/jbc.M111.269225","article-title":"Structure and function of papiliocin with antimicrobial and anti-inflammatory activities isolated from the swallowtail butterfly, Papilio xuthus","volume":"286","author":"Kim","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"12048","DOI":"10.1038\/srep12048","article-title":"Functional roles of aromatic residues and helices of papiliocin in its antimicrobial and anti-inflammatory activities","volume":"5","author":"Lee","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_59","first-page":"457","article-title":"Purification and Characterization of Antibacterial Peptides, Spodopsin Ia and Ib Induced in the Larval Haemolymph of the Common Cutworm, Spodoptera Iitura","volume":"1","author":"Choi","year":"1997","journal-title":"Korean J. Biol. Sci."},{"key":"ref_60","first-page":"287","article-title":"Antibacterial properties and partial cDNA sequences of cecropin-like antibacterial peptides from the common cutworm, Spodoptera litura","volume":"125","author":"Choi","year":"2000","journal-title":"Comp. Biochem. Physiol. C Toxicol. Pharmacol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.cbpb.2007.07.010","article-title":"Characterization and expression of a cecropin-like gene from Helicoverpa armigera","volume":"148","author":"Wang","year":"2007","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1111\/j.1432-1033.1996.00263.x","article-title":"Formation of pores in Escherichia coli cell membranes by a cecropin isolated from hemolymph of Heliothis virescens larvae","volume":"236","author":"Lockey","year":"1996","journal-title":"Eur. J. Biochem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1002\/1520-6327(200012)45:4<149::AID-ARCH2>3.0.CO;2-H","article-title":"cDNA cloning and antibacterial activities of cecropin D-like peptides from Agrius convolvuli","volume":"45","author":"Kim","year":"2000","journal-title":"Arch. Insect Biochem. Physiol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1080\/19768354.2013.769465","article-title":"Expression, cDNA cloning, and characterization of the antibacterial peptide cecropin D from Agrius convolvuli","volume":"17","author":"Park","year":"2013","journal-title":"Anim. Cells Syst."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/S1016-8478(23)13329-2","article-title":"Hinnavin I, an antibacterial peptide from cabbage butterfly, Artogeia rapae","volume":"7","author":"Bang","year":"1997","journal-title":"Mol. Cells"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.cbpb.2006.02.010","article-title":"Characterization and cDNA cloning of hinnavin II, a cecropin family antibacterial peptide from the cabbage butterfly, Artogeia rapae","volume":"144","author":"Yoe","year":"2006","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.peptides.2018.01.017","article-title":"Identification and screening of potent antimicrobial peptides in arthropod genomes","volume":"103","author":"Duwadi","year":"2018","journal-title":"Peptides"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1002\/j.1460-2075.1990.tb08098.x","article-title":"The cecropin locus in Drosophila; a compact gene cluster involved in the response to infection","volume":"9","author":"Kylsten","year":"1990","journal-title":"EMBO J."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1111\/j.1432-1033.1992.tb16648.x","article-title":"CecC, a cecropin gene expressed during metamorphosis in Drosophila pupae","volume":"204","author":"Tryselius","year":"1992","journal-title":"Eur. J. Biochem."},{"key":"ref_70","first-page":"857","article-title":"Rapid expansion of immune-related gene families in the house fly, Musca domestica","volume":"34","author":"Sackton","year":"2017","journal-title":"Mol. Biol. Evol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"11510","DOI":"10.1016\/S0021-9258(18)98986-6","article-title":"The cecropin locus. Cloning and expression of a gene cluster encoding three antibacterial peptides in Hyalophora cecropia","volume":"266","author":"Gudmundsson","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"97","DOI":"10.6026\/97320630005097","article-title":"Molecular evolution of the cecropin multigene family in silkworm Bombyx mori","volume":"5","author":"Ponnuvel","year":"2010","journal-title":"Bioinformation"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"101989","DOI":"10.1155\/2012\/101989","article-title":"Coleopteran antimicrobial peptides: Prospects for clinical applications","volume":"2012","author":"Ntwasa","year":"2012","journal-title":"Int. J. Microbiol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"R177","DOI":"10.1186\/gb-2007-8-8-r177","article-title":"Comparative genomic analysis of the Tribolium immune system","volume":"8","author":"Zou","year":"2007","journal-title":"Genome Biol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00239-004-0053-4","article-title":"Birth-and-death evolution of the Cecropin multigene family in Drosophila","volume":"60","author":"Quesada","year":"2005","journal-title":"J. Mol. Evol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/j.dci.2014.05.020","article-title":"Sequence diversity and evolution of antimicrobial peptides in invertebrates","volume":"48","author":"Tassanakajon","year":"2015","journal-title":"Dev. Comp. Immunol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1093\/genetics\/150.1.157","article-title":"Molecular evolution of the cecropin multigene family in Drosophila: Functional genes vs. pseudogenes","volume":"150","author":"Aguade","year":"1998","journal-title":"Genetics"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"20150291","DOI":"10.1098\/rstb.2015.0291","article-title":"The potential for adaptive maintenance of diversity in insect antimicrobial peptides","volume":"371","author":"Unckless","year":"2016","journal-title":"Phil. Tran. R. Soc. B"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.1111\/j.1420-9101.2005.00925.x","article-title":"Molecular evolution of animal antimicrobial peptides: Widespread moderate positive selection","volume":"18","author":"Tennessen","year":"2005","journal-title":"J. Evol. Biol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.3892\/ijo.2015.2933","article-title":"CecropinXJ inhibits the proliferation of human gastric cancer BGC823 cells and induces cell death in vitro and in vivo","volume":"46","author":"Wu","year":"2015","journal-title":"Int. J. Oncol."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Price, M.N., Dehal, P.S., and Arkin, A.P. (2010). FastTree 2\u2013approximately maximum-likelihood trees for large alignments. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0009490"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/j.tig.2007.05.003","article-title":"A multilayered defense against infection: Combinatorial control of insect immune genes","volume":"23","author":"Uvell","year":"2007","journal-title":"Trends Genet."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1038\/s41598-017-01162-z","article-title":"Differential sensitivity to infections and antimicrobial peptide-mediated immune response in four silkworm strains with different geographical origin","volume":"7","author":"Romoli","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1016\/j.bbamem.2006.02.021","article-title":"Peptide\u2013membrane interactions and mechanisms of membrane destruction by amphipathic \u03b1-helical antimicrobial peptides","volume":"1758","author":"Sato","year":"2006","journal-title":"Biochim. Biophys. Acta."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"7884","DOI":"10.1021\/la501549v","article-title":"Channel-forming activity of cecropins in lipid bilayers: Effect of agents modifying the membrane dipole potential","volume":"30","author":"Efimova","year":"2014","journal-title":"Langmuir"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1134\/S1990519X18040028","article-title":"Regulation of the Pore-Forming Activity of Cecropin A by Local Anesthetics","volume":"12","author":"Efimova","year":"2018","journal-title":"Cell Tiss. Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1124\/pr.55.1.2","article-title":"Mechanisms of antimicrobial peptide action and resistance","volume":"55","author":"Yeaman","year":"2003","journal-title":"Pharmacol. Rev."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1683","DOI":"10.1021\/bi00328a017","article-title":"N-terminal analogs of cecropin A: Synthesis, antibacterial activity, and conformational properties","volume":"24","author":"Andreu","year":"1985","journal-title":"Biochemistry"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"5072","DOI":"10.1073\/pnas.85.14.5072","article-title":"Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes","volume":"85","author":"Christensen","year":"1988","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1623","DOI":"10.1016\/S0006-3495(92)81730-7","article-title":"Modeling the ion channel structure of cecropin","volume":"63","author":"Durell","year":"1992","journal-title":"Biophys. J."},{"key":"ref_91","unstructured":"Tacconelli, E., Magrini, N., Kahlmeter, G., and Singh, N. (2017). Global Priority List of Antibiotic-Resistant Bacteria to Guide Research, Discovery, and Development of New Antibiotics, World Health Organization."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"2878","DOI":"10.1096\/fasebj.2.13.3049204","article-title":"In vitro cytocidal effect of novel lytic peptides on Plasmodium falciparum and Trypanosoma cruzi","volume":"2","author":"Jaynes","year":"1988","journal-title":"FASEB J."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1080\/mmy.38.4.301.308","article-title":"D-cecropin B: Proteolytic resistance, lethality for pathogenic fungi and binding properties","volume":"38","author":"Bland","year":"2000","journal-title":"Med. Mycol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0014-5793(89)81505-4","article-title":"Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids","volume":"259","author":"Boman","year":"1989","journal-title":"FEBS Lett."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1128\/AAC.50.4.1251-1256.2006","article-title":"Activity of cecropin A-melittin hybrid peptides against colistin-resistant clinical strains of Acinetobacter baumannii: Molecular basis for the differential mechanisms of action","volume":"50","author":"Saugar","year":"2006","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1080\/21505594.2016.1213475","article-title":"Activity of antimicrobial peptides, alone or combined with conventional antibiotics, against Staphylococcus aureus isolated from the airways of cystic fibrosis patients","volume":"8","author":"Garbacz","year":"2017","journal-title":"Virulence"},{"key":"ref_97","doi-asserted-by":"crossref","unstructured":"Geitani, R., Moubareck, C.A., Touqui, L., and Sarkis, D.K. (2019). Cationic antimicrobial peptides: Alternatives and\/or adjuvants to antibiotics active against methicillin-resistant Staphylococcus aureus and multidrug-resistant Pseudomonas aeruginosa. BMC Microbiol., 19.","DOI":"10.1186\/s12866-019-1416-8"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1016\/j.bbrc.2014.08.044","article-title":"Cecropin A\u2013melittin mutant with improved proteolytic stability and enhanced antimicrobial activity against bacteria and fungi associated with gastroenteritis in vitro","volume":"451","author":"Ji","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"2441","DOI":"10.1128\/AAC.45.9.2441-2449.2001","article-title":"N-terminal fatty acid substitution increases the leishmanicidal activity of CA (1-7) M (2-9), a cecropin-melittin hybrid peptide","volume":"45","author":"Chicharro","year":"2001","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1111\/j.1399-3011.1997.tb01469.x","article-title":"Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides","volume":"50","author":"Shin","year":"1997","journal-title":"J. Pept. Res."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"11855","DOI":"10.1021\/bi000453g","article-title":"Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A (1\u20138)\u2013magainin 2 (1\u201312) and its analogues, on their antibiotic activities and structures","volume":"39","author":"Oh","year":"2000","journal-title":"Biochemistry"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1839","DOI":"10.5012\/bkcs.2009.30.8.1839","article-title":"Antibacterial activity and synergism of the hybrid antimicrobial peptide, CAMA-syn","volume":"30","author":"Jeong","year":"2009","journal-title":"Bull. Korean Chem. Soc."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1677","DOI":"10.1038\/jid.2011.112","article-title":"Antimicrobial and anti-inflammatory effects of Cecropin A(1\u20138)-Magainin2(1\u201312) hybrid peptide analog p5 against Malassezia furfur infection in human keratinocytes","volume":"131","author":"Ryu","year":"2011","journal-title":"J. Invest. Dermatol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1002\/psc.504","article-title":"Structure-antiviral activity relationships of cecropin A-magainin 2 hybrid peptide and its analogues","volume":"10","author":"Lee","year":"2004","journal-title":"J. Pept. Sci."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1128\/AAC.01998-15","article-title":"Antimicrobial Peptide CMA3 Derived from the CA-MA Hybrid Peptide: Antibacterial and Anti-inflammatory Activities with Low Cytotoxicity and Mechanism of Action in Escherichia coli","volume":"60","author":"Lee","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Wei, X.-B., Wu, R.-J., Si, D.-Y., Liao, X.-D., Zhang, L.-L., and Zhang, R.-J. (2016). Novel hybrid peptide cecropin A (1\u20138)-LL37 (17\u201330) with potential antibacterial activity. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17070983"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1016\/j.foodchem.2016.09.033","article-title":"A potential food biopreservative, CecXJ-37N, non-covalently intercalates into the nucleotides of bacterial genomic DNA beyond membrane attack","volume":"217","author":"Liu","year":"2017","journal-title":"Food Chem."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1186\/s13071-015-1149-y","article-title":"A potent anti-inflammatory peptide from the salivary glands of horsefly","volume":"8","author":"Wei","year":"2015","journal-title":"Parasites Vectors."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1016\/j.aninu.2018.04.006","article-title":"Animals as sources of food-borne pathogens: A review","volume":"4","author":"Heredia","year":"2018","journal-title":"Anim. Nutr."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"2173","DOI":"10.3389\/fmicb.2016.02173","article-title":"Azole antifungal resistance in Candida albicans and emerging non-albicans Candida species","volume":"7","author":"Whaley","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"7204","DOI":"10.18632\/oncotarget.23208","article-title":"Inflammatory responses and inflammation-associated diseases in organs","volume":"9","author":"Chen","year":"2017","journal-title":"Oncotarget"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.1039\/c5ib00158g","article-title":"On the translocation of bacteria and their lipopolysaccharides between blood and peripheral locations in chronic, inflammatory diseases: The central roles of LPS and LPS-induced cell death","volume":"7","author":"Kell","year":"2015","journal-title":"Integr. Biol. (Camb.)"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"3817","DOI":"10.1038\/s41598-019-40577-8","article-title":"Development of a novel short 12-meric papiliocin-derived peptide that is effective against Gram-negative sepsis","volume":"9","author":"Kim","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1666","DOI":"10.1097\/00003246-200109000-00002","article-title":"Effect of mono-dose intraperitoneal cecropins in experimental septic shock","volume":"29","author":"Giacometti","year":"2001","journal-title":"Crit. Care Med."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"522","DOI":"10.3389\/fmicb.2019.00522","article-title":"Musca domestica Cecropin (Mdc) Alleviates Salmonella typhimurium-Induced Colonic Mucosal Barrier Impairment: Associating With Inflammatory and Oxidative Stress Response, Tight Junction as Well as Intestinal Flora","volume":"10","author":"Zhang","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0304-4165(97)00024-X","article-title":"Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria, and cancer cells","volume":"1336","author":"Chen","year":"1997","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_117","first-page":"265","article-title":"Preliminary experimental anticancer activity of cecropins","volume":"7","author":"Moore","year":"1994","journal-title":"Pept. Res."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"831709","DOI":"10.1155\/2013\/831709","article-title":"The cytotoxic effect of magainin II on the MDA-MB-231 and M14K tumour cell lines","volume":"2013","author":"Anghel","year":"2013","journal-title":"Biomed. Res. Int."},{"key":"ref_119","first-page":"4467","article-title":"Enhancement of the cytolytic effect of anti-bacterial cecropin by the microvilli of cancer cells","volume":"18","author":"Chan","year":"1998","journal-title":"Anticancer Res."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1093\/abbs\/gmq021","article-title":"Apoptosis-inducing activity of the antimicrobial peptide cecropin of Musca domestica in human hepatocellular carcinoma cell line BEL-7402 and the possible mechanism","volume":"42","author":"Jin","year":"2010","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1186\/1471-2490-8-5","article-title":"Antimicrobial peptides of the Cecropin-family show potent antitumor activity against bladder cancer cells","volume":"8","author":"Suttmann","year":"2008","journal-title":"BMC Urol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1007\/978-981-13-3588-4_9","article-title":"Anticancer Activities of Natural and Synthetic Peptides","volume":"Volume 1117","author":"Matsuzaki","year":"2019","journal-title":"Antimicrobial Peptides. Advances in Experimental Medicine and Biology"},{"key":"ref_123","first-page":"6245","article-title":"Therapeutic effects of antimicrobial peptide on malignant ascites in a mouse model","volume":"17","author":"Xia","year":"2018","journal-title":"Mol. Med. Rep."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"49","DOI":"10.2147\/IDR.S55778","article-title":"Agriculture and food animals as a source of antimicrobial-resistant bacteria","volume":"8","author":"Economou","year":"2015","journal-title":"Infect. Drug Resist."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"87","DOI":"10.22358\/jafs\/69998\/2017","article-title":"Insect proteins as a potential source of antimicrobial peptides in livestock production. A review","volume":"26","author":"Jozefiak","year":"2017","journal-title":"J. Anim. Feed Sci."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1007\/s10126-013-9550-z","article-title":"Production of homozygous transgenic rainbow trout with enhanced disease resistance","volume":"16","author":"Chiou","year":"2014","journal-title":"Mar. Biotechnol."},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Bund\u00f3, M., Montesinos, L., Izquierdo, E., Campo, S., Mieulet, D., Guiderdoni, E., Rossignol, M., Badosa, E., Montesinos, E., and San Segundo, B. (2014). Production of cecropin A antimicrobial peptide in rice seed endosperm. BMC Plant Biol., 14.","DOI":"10.1186\/1471-2229-14-102"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"461","DOI":"10.4103\/0976-237X.169846","article-title":"Assessment of salivary calcium, phosphate, magnesium, pH, and flow rate in healthy subjects, periodontitis, and dental caries","volume":"6","author":"Rajesh","year":"2015","journal-title":"Contemp. Clin. Dent."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1633","DOI":"10.1164\/ajrccm\/148.6_Pt_1.1633","article-title":"Elemental composition of human airway surface fluid in healthy and diseased airways","volume":"148","author":"Joris","year":"1993","journal-title":"Am. Rev. Respir. Dis."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Shrestha, A., Duwadi, D., Jukosky, J., and Fiering, S.N. (2019). Cecropin-like antimicrobial peptide protects mice from lethal E. coli infection. PLoS ONE, 14.","DOI":"10.1371\/journal.pone.0220344"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1007\/s12602-018-9465-0","article-title":"Antimicrobial Peptides: The Achilles\u2019 Heel of Antibiotic Resistance?","volume":"11","author":"Lewies","year":"2019","journal-title":"Probiotics Antimicrob. Proteins"},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Rodr\u00edguez-Rojas, A., Makarova, O., and Rolff, J. (2014). Antimicrobials, stress and mutagenesis. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1004445"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"2409","DOI":"10.3389\/fmicb.2017.02409","article-title":"Combination strategies to enhance the efficacy of antimicrobial peptides against bacterial biofilms","volume":"8","author":"Grassi","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.peptides.2014.09.021","article-title":"Inhibition and destruction of Pseudomonas aeruginosa biofilms by antibiotics and antimicrobial peptides","volume":"62","author":"Dosler","year":"2014","journal-title":"Peptides"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1038\/nrmicro.2016.94","article-title":"Biofilms: An emergent form of bacterial life","volume":"14","author":"Flemming","year":"2016","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1159\/000491497","article-title":"Design and assessment of anti-biofilm peptides: Steps toward clinical application","volume":"11","author":"Dostert","year":"2019","journal-title":"J. Innate Immun."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"63","DOI":"10.3389\/fchem.2017.00063","article-title":"Antimicrobial peptides in biomedical device manufacturing","volume":"5","author":"Riool","year":"2017","journal-title":"Front. Chem."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"6366","DOI":"10.1128\/AAC.01180-12","article-title":"In vitro activities of antibiotics and antimicrobial cationic peptides alone and in combination against methicillin-resistant Staphylococcus aureus biofilms","volume":"56","author":"Mataraci","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1894","DOI":"10.1021\/acsbiomaterials.6b00266","article-title":"Bactericidal Hydrogels via Surface Functionalization with Cecropin A","volume":"2","author":"Cole","year":"2016","journal-title":"ACS Biomater. Sci. Eng."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"1801390","DOI":"10.1002\/admi.201801390","article-title":"Cecropin\u2013Melittin Functionalized Polyurethane Surfaces Prevent Staphylococcus epidermidis Adhesion without Inducing Platelet Adhesion and Activation","volume":"5","author":"Querido","year":"2018","journal-title":"Adv. Mater. Interfaces"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"2988","DOI":"10.1016\/j.apsusc.2007.10.049","article-title":"Surface modification and properties of Bombyx mori silk fibroin films by antimicrobial peptide","volume":"254","author":"Bai","year":"2008","journal-title":"Appl. Surf. Sci."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1007\/s11248-018-0059-0","article-title":"Intrinsic antimicrobial properties of silk spun by genetically modified silkworm strains","volume":"27","author":"Saviane","year":"2018","journal-title":"Transgenic Res."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"855","DOI":"10.3389\/fmicb.2018.00855","article-title":"Antimicrobial peptides and nanotechnology, recent advances and challenges","volume":"9","author":"Biswaro","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.biomaterials.2016.01.051","article-title":"One-step synthesis of high-density peptide-conjugated gold nanoparticles with antimicrobial efficacy in a systemic infection model","volume":"85","author":"Rai","year":"2016","journal-title":"Biomaterials"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.3389\/fmicb.2018.01048","article-title":"Recent progress in the chemical synthesis of class II and S-glycosylated bacteriocins","volume":"9","author":"Biron","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1377\/hlthaff.2017.1153","article-title":"Antibiotic-resistant infection treatment costs have doubled since 2002, now exceeding $2 billion annually","volume":"37","author":"Thorpe","year":"2018","journal-title":"Health Affairs"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/20\/23\/5862\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T13:36:45Z","timestamp":1760189805000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/20\/23\/5862"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,11,22]]},"references-count":146,"journal-issue":{"issue":"23","published-online":{"date-parts":[[2019,12]]}},"alternative-id":["ijms20235862"],"URL":"https:\/\/doi.org\/10.3390\/ijms20235862","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,11,22]]}}}