{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T23:35:13Z","timestamp":1793403313321,"version":"4.5.0"},"reference-count":161,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2022,10,16]],"date-time":"2022-10-16T00:00:00Z","timestamp":1665878400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antibiotics"],"abstract":"<jats:p>The growing emergence of antimicrobial resistance represents a global problem that not only influences healthcare systems but also has grave implications for political and economic processes. As the discovery of novel antimicrobial agents is lagging, one of the solutions is innovative therapeutic options that would expand our armamentarium against this hazard. Compounds of interest in many such studies are antimicrobial peptides (AMPs), which actually represent the host\u2019s first line of defense against pathogens and are involved in innate immunity. They have a broad range of antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, and viruses, with specific mechanisms of action utilized by different AMPs. Coupled with a lower propensity for resistance development, it is becoming clear that AMPs can be seen as emerging and very promising candidates for more pervasive usage in the treatment of infectious diseases. However, their use in quotidian clinical practice is not without challenges. In this review, we aimed to summarize state-of-the-art evidence on the structure and mechanisms of action of AMPs, as well as to provide detailed information on their antimicrobial activity. We also aimed to present contemporary evidence of clinical trials and application of AMPs and highlight their use beyond infectious diseases and potential challenges that may arise with their increasing availability.<\/jats:p>","DOI":"10.3390\/antibiotics11101417","type":"journal-article","created":{"date-parts":[[2022,10,16]],"date-time":"2022-10-16T21:10:10Z","timestamp":1665954610000},"page":"1417","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":282,"title":["Antimicrobial Peptides\u2014Mechanisms of Action, Antimicrobial Effects and Clinical Applications"],"prefix":"10.3390","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5957-0807","authenticated-orcid":false,"given":"Jasminka","family":"Talapko","sequence":"first","affiliation":[{"name":"Faculty of Dental Medicine and Health, Josip Juraj Strossmayer University of Osijek, 31000 Osijek, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tomislav","family":"Me\u0161trovi\u0107","sequence":"additional","affiliation":[{"name":"University Centre Vara\u017edin, University North, 42000 Vara\u017edin, Croatia"},{"name":"Institute for Health Metrics and Evaluation, University of Washington, 3980 15th Ave. NE, Seattle, WA 98195, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9211-6251","authenticated-orcid":false,"given":"Martina","family":"Juzba\u0161i\u0107","sequence":"additional","affiliation":[{"name":"Faculty of Dental Medicine and Health, Josip Juraj Strossmayer University of Osijek, 31000 Osijek, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7933-3371","authenticated-orcid":false,"given":"Matej","family":"Tomas","sequence":"additional","affiliation":[{"name":"Faculty of Dental Medicine and Health, Josip Juraj Strossmayer University of Osijek, 31000 Osijek, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suzana","family":"Eri\u0107","sequence":"additional","affiliation":[{"name":"Faculty of Medicine, Josip Juraj Strossmayer University of Osijek, Josipa Huttlera 4, 31000 Osijek, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lorena","family":"Horvat Aleksijevi\u0107","sequence":"additional","affiliation":[{"name":"Faculty of Dental Medicine and Health, Josip Juraj Strossmayer University of Osijek, 31000 Osijek, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sanja","family":"Beki\u0107","sequence":"additional","affiliation":[{"name":"Faculty of Medicine, Josip Juraj Strossmayer University of Osijek, Josipa Huttlera 4, 31000 Osijek, Croatia"},{"name":"Family Medicine Practice, 31000 Osijek, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dragan","family":"Schwarz","sequence":"additional","affiliation":[{"name":"Faculty of Dental Medicine and Health, Josip Juraj Strossmayer University of Osijek, 31000 Osijek, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suzana","family":"Mati\u0107","sequence":"additional","affiliation":[{"name":"Faculty of Medicine, Josip Juraj Strossmayer University of Osijek, Josipa Huttlera 4, 31000 Osijek, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marijana","family":"Neuberg","sequence":"additional","affiliation":[{"name":"University Centre Vara\u017edin, University North, 42000 Vara\u017edin, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1842-930X","authenticated-orcid":false,"given":"Ivana","family":"\u0160krlec","sequence":"additional","affiliation":[{"name":"Faculty of Dental Medicine and Health, Josip Juraj Strossmayer University of Osijek, 31000 Osijek, Croatia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,10,16]]},"reference":[{"key":"ref_1","first-page":"3919","article-title":"The antimicrobial peptides and their potential clinical applications","volume":"11","author":"Lei","year":"2019","journal-title":"Am. J. Transl. Res."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Talapko, J., and \u0160krlec, I. (2020). The Principles, Mechanisms, and Benefits of Unconventional Agents in the Treatment of Biofilm Infection. Pharmaceuticals, 13.","DOI":"10.3390\/ph13100299"},{"key":"ref_3","first-page":"2049936121991374","article-title":"Climate change and antibiotic resistance: A deadly combination","volume":"8","author":"Burnham","year":"2021","journal-title":"Ther. Adv. Infect. Dis."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"849","DOI":"10.2147\/IDR.S289741","article-title":"Evidence of Antibiotic Resistance from Population-Based Studies: A Narrative Review","volume":"14","author":"Giacomini","year":"2021","journal-title":"Infect. Drug Resist."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1016\/S0140-6736(21)02724-0","article-title":"Global burden of bacterial antimicrobial resistance in 2019: A systematic analysis","volume":"399","author":"Murray","year":"2022","journal-title":"Lancet"},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Bhattacharjya, S., Mohid, S.A., and Bhunia, A. (2022). Atomic-Resolution Structures and Mode of Action of Clinically Relevant Antimicrobial Peptides. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23094558"},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Shaka, M., Arias-Rojas, A., Hrdina, A., Frahm, D., and Iatsenko, I. (2022). Lipopolysaccharide-mediated resistance to host antimicrobial peptides and hemocyte-derived reactive-oxygen species are the major Providencia alcalifaciens virulence factors in Drosophila melanogaster. PLoS Pathog., 18.","DOI":"10.1101\/2022.05.17.492247"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Bhattacharjya, S., and Straus, S.K. (2020). Design, Engineering and Discovery of Novel \u03b1-Helical and \u03b2-Boomerang Antimicrobial Peptides against Drug Resistant Bacteria. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21165773"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Ghimire, J., Guha, S., Nelson, B.J., Morici, L.A., and Wimley, W.C. (J. Membr. Biol., 2022). The Remarkable Innate Resistance of Burkholderia bacteria to Cationic Antimicrobial Peptides: Insights into the Mechanism of AMP Resistance, J. Membr. Biol., in press.","DOI":"10.1007\/s00232-022-00232-2"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"7820","DOI":"10.1039\/D0CS00729C","article-title":"The multifaceted nature of antimicrobial peptides: Current synthetic chemistry approaches and future directions","volume":"50","author":"Gan","year":"2021","journal-title":"Chem. Soc. Rev."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1186\/s13223-018-0278-1","article-title":"An introduction to immunology and immunopathology","volume":"14","author":"Marshall","year":"2018","journal-title":"Allergy Asthma. Clin. Immunol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/j.ijantimicag.2004.09.005","article-title":"Antimicrobial peptides: Premises and promises","volume":"24","author":"Reddy","year":"2004","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"582779","DOI":"10.3389\/fmicb.2020.582779","article-title":"Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields","volume":"11","author":"Huan","year":"2020","journal-title":"Front. Microbiol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1669","DOI":"10.3389\/fmicb.2020.01669","article-title":"The Demand for New Antibiotics: Antimicrobial Peptides, Nanoparticles, and Combinatorial Therapies as Future Strategies in Antibacterial Agent Design","volume":"11","year":"2020","journal-title":"Front. Microbiol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1038\/s41579-021-00649-x","article-title":"Antibiotic resistance in the environment","volume":"20","author":"Larsson","year":"2022","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/s41577-020-00479-7","article-title":"A guide to vaccinology: From basic principles to new developments","volume":"21","author":"Pollard","year":"2021","journal-title":"Nat. Rev. Immunol."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Lachowicz, J.I., Szczepski, K., Scano, A., Casu, C., Fais, S., Orr\u00f9, G., Pisano, B., Piras, M., and Jaremko, M. (2020). The Best Peptidomimetic Strategies to Undercover Antibacterial Peptides. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21197349"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1139\/cjm-2020-0142","article-title":"d-Amino acids in antimicrobial peptides: A potential approach to treat and combat antimicrobial resistance","volume":"67","author":"Kapil","year":"2021","journal-title":"Can. J. Microbiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"668632","DOI":"10.3389\/fcimb.2021.668632","article-title":"Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields","volume":"11","author":"Moretta","year":"2021","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Mishra, A.K., Choi, J., Moon, E., and Baek, K.H. (2018). Tryptophan-Rich and Proline-Rich Antimicrobial Peptides. Molecules, 23.","DOI":"10.3390\/molecules23040815"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"691532","DOI":"10.3389\/fchem.2021.691532","article-title":"Antimicrobial Peptides and Proteins: From Nature\u2019s Reservoir to the Laboratory and Beyond","volume":"9","author":"Sarkar","year":"2021","journal-title":"Front. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"194","DOI":"10.3389\/fcimb.2016.00194","article-title":"Antimicrobial peptides: An emerging category of therapeutic agents","volume":"6","author":"Mahlapuu","year":"2016","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Rima, M., Rima, M., Fajloun, Z., Sabatier, J.M., Bechinger, B., and Naas, T. (2021). Antimicrobial Peptides: A Potent Alternative to Antibiotics. Antibiotics, 10.","DOI":"10.3390\/antibiotics10091095"},{"key":"ref_24","first-page":"48","article-title":"Antimicrobial peptides: Mechanism of action, activity and clinical potential","volume":"8","author":"Zhang","year":"2021","journal-title":"Mil. Med. Res."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"4710","DOI":"10.1038\/s41598-020-61526-w","article-title":"Chiral supramolecular architecture of stable transmembrane pores formed by an \u03b1-helical antibiotic peptide in the presence of lyso-lipids","volume":"10","author":"Strandberg","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"9117","DOI":"10.1038\/s41598-020-65688-5","article-title":"A novel, rationally designed, hybrid antimicrobial peptide, inspired by cathelicidin and aurein, exhibits membrane-active mechanisms against Pseudomonas aeruginosa","volume":"10","author":"Klubthawee","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"e02340-16","DOI":"10.1128\/AAC.02340-16","article-title":"Intracellular Targeting Mechanisms by Antimicrobial Peptides","volume":"61","author":"Le","year":"2017","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"17795","DOI":"10.1038\/s41598-017-18102-6","article-title":"Structure and Interactions of A Host Defense Antimicrobial Peptide Thanatin in Lipopolysaccharide Micelles Reveal Mechanism of Bacterial Cell Agglutination","volume":"7","author":"Sinha","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"204","DOI":"10.3389\/fchem.2018.00204","article-title":"Antimicrobial Peptides: Interaction with Model and Biological Membranes and Synergism with Chemical Antibiotics","volume":"6","author":"Hollmann","year":"2018","journal-title":"Front. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"18328","DOI":"10.1038\/s41598-021-97779-2","article-title":"Interplay between membrane active host defense peptides and heme modulates their assemblies and in vitro activity","volume":"11","author":"Ricci","year":"2021","journal-title":"Sci. Rep."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"e12193","DOI":"10.7717\/peerj.12193","article-title":"The characteristics and roles of antimicrobial peptides as potential treatment for antibiotic-resistant pathogens: A review","volume":"9","author":"Gopalsamy","year":"2021","journal-title":"PeerJ"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"609542","DOI":"10.3389\/fcimb.2021.609542","article-title":"Overlapping Properties of the Short Membrane-Active Peptide BP100 with (i) Polycationic TAT and (ii) \u03b1-helical Magainin Family Peptides","volume":"11","author":"Mink","year":"2021","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Zhang, S., Ma, M., Shao, Z., Zhang, J., Fu, L., Li, X., Fang, W., and Gao, L. (2021). Structure and Formation Mechanism of Antimicrobial Peptides Temporin B- and L-Induced Tubular Membrane Protrusion. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222011015"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1089\/mdr.2017.0392","article-title":"Antimicrobial Peptides: Features, Action, and Their Resistance Mechanisms in Bacteria","volume":"24","author":"Moravej","year":"2018","journal-title":"Microb. Drug Resist."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1046\/j.1365-2796.2003.01228.x","article-title":"Antibacterial peptides: Basic facts and emerging concepts","volume":"254","author":"Boman","year":"2003","journal-title":"J. Intern. Med."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1038\/nrd3591","article-title":"Designing antimicrobial peptides: Form follows function","volume":"11","author":"Fjell","year":"2011","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Luo, Y., and Song, Y. (2021). Mechanism of Antimicrobial Peptides: Antimicrobial, Anti-Inflammatory and Antibiofilm Activities. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222111401"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1128\/CMR.16.4.673-687.2003","article-title":"Bacterial wall as target for attack: Past, present, and future research","volume":"16","author":"Koch","year":"2003","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3062","DOI":"10.1016\/j.bbamem.2015.04.014","article-title":"Structural variations of the cell wall precursor lipid II in Gram-positive bacteria\u2014Impact on binding and efficacy of antimicrobial peptides","volume":"1848","author":"Sahl","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"E1409","DOI":"10.1073\/pnas.1319900111","article-title":"Small cationic antimicrobial peptides delocalize peripheral membrane proteins","volume":"111","author":"Wenzel","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_41","first-page":"2006","article-title":"A New Synthetic Peptide Having Two Target of Antibacterial Action in E. coli ML35","volume":"7","author":"Curtidor","year":"2016","journal-title":"Front. Microbiol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/978-1-4939-6737-7_1","article-title":"Antimicrobial Peptides: An Introduction","volume":"1548","author":"Haney","year":"2017","journal-title":"Methods Mol. Biol."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Di Somma, A., Moretta, A., Can\u00e8, C., Cirillo, A., and Duilio, A. (2020). Antimicrobial and Antibiofilm Peptides. Biomolecules, 10.","DOI":"10.3390\/biom10040652"},{"key":"ref_44","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_45","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.jcis.2018.10.103","article-title":"Membrane targeting cationic antimicrobial peptides","volume":"537","author":"Ciumac","year":"2019","journal-title":"J. Colloid Interface Sci."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1016\/j.drudis.2012.03.002","article-title":"Cell-penetrating peptides: Classes, origin, and current landscape","volume":"17","author":"Milletti","year":"2012","journal-title":"Drug Discov. Today"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/nrmicro1098","article-title":"Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?","volume":"3","author":"Brogden","year":"2005","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1007\/978-981-13-3588-4_7","article-title":"Antimicrobial and Cell-Penetrating Peptides: How to Understand Two Distinct Functions Despite Similar Physicochemical Properties","volume":"1117","author":"Neundorf","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1128\/AAC.01619-12","article-title":"Two hits are better than one: Membrane-active and DNA binding-related double-action mechanism of NK-18, a novel antimicrobial peptide derived from mammalian NK-lysin","volume":"57","author":"Yan","year":"2013","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.micpath.2018.11.052","article-title":"Antibacterial and anti-biofilm activity, and mechanism of action of pleurocidin against drug resistant Staphylococcus aureus","volume":"127","author":"Ko","year":"2019","journal-title":"Microb. Pathog."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/j.ijmm.2009.08.017","article-title":"The synthesis and function of the alarmone (p)ppGpp in firmicutes","volume":"300","author":"Wolz","year":"2010","journal-title":"Int. J. Med. Microbiol."},{"key":"ref_52","first-page":"251","article-title":"Bacterial evasion of antimicrobial peptides by biofilm formation","volume":"306","author":"Otto","year":"2006","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1021\/acsptsci.0c00081","article-title":"Potential Role of Peptide-Based Antiviral Therapy against SARS-CoV-2 Infection","volume":"3","author":"Maiti","year":"2020","journal-title":"ACS Pharmacol. Transl. Sci."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Li, X., Zuo, S., Wang, B., Zhang, K., and Wang, Y. (2022). Antimicrobial Mechanisms and Clinical Application Prospects of Antimicrobial Peptides. Molecules, 27.","DOI":"10.3390\/molecules27092675"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Ahmed, A., Siman-Tov, G., Hall, G., Bhalla, N., and Narayanan, A. (2019). Human Antimicrobial Peptides as Therapeutics for Viral Infections. Viruses, 11.","DOI":"10.3390\/v11080704"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"3525","DOI":"10.1007\/s00018-019-03138-w","article-title":"Antiviral peptides as promising therapeutic drugs","volume":"76","author":"Campos","year":"2019","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"5428","DOI":"10.3390\/v7102883","article-title":"Perspective of Use of Antiviral Peptides against Influenza Virus","volume":"7","author":"Skalickova","year":"2015","journal-title":"Viruses"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1080\/19490976.2017.1405209","article-title":"Modulation of the gut microbiota by metformin improves metabolic profiles in aged obese mice","volume":"9","author":"Lee","year":"2018","journal-title":"Gut Microbes"},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Barlow, P.G., Svoboda, P., Mackellar, A., Nash, A.A., York, I.A., Pohl, J., Davidson, D.J., and Donis, R.O. (2011). Antiviral activity and increased host defense against influenza infection elicited by the human cathelicidin LL-37. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0025333"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1785802","DOI":"10.1080\/19490976.2020.1785802","article-title":"Cathelicidin-mediated lipopolysaccharide signaling via intracellular TLR4 in colonic epithelial cells evokes CXCL8 production","volume":"12","author":"Holani","year":"2020","journal-title":"Gut Microbes"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.antiviral.2014.01.015","article-title":"A new class of synthetic anti-lipopolysaccharide peptides inhibits influenza A virus replication by blocking cellular attachment","volume":"104","author":"Hoffmann","year":"2014","journal-title":"Antiviral Res."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"5145","DOI":"10.1016\/j.bmc.2005.05.051","article-title":"Antiviral cyclic D,L-alpha-peptides: Targeting a general biochemical pathway in virus infections","volume":"13","author":"Horne","year":"2005","journal-title":"Bioorg. Med. Chem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"321","DOI":"10.3389\/fmicb.2013.00321","article-title":"Current scenario of peptide-based drugs: The key roles of cationic antitumor and antiviral peptides","volume":"4","author":"Mulder","year":"2013","journal-title":"Front. Microbiol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1016\/j.ijantimicag.2003.07.022","article-title":"Antiviral activity of antimicrobial cationic peptides against Junin virus and herpes simplex virus","volume":"23","author":"Castilla","year":"2004","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"722","DOI":"10.3389\/fimmu.2018.00722","article-title":"Cathelicidin-derived antimicrobial peptides inhibit Zika virus through direct inactivation and interferon pathway","volume":"9","author":"He","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_66","doi-asserted-by":"crossref","unstructured":"Bakovic, A., Risner, K., Bhalla, N., Alem, F., Chang, T.L., Weston, W., Harness, J.A., and Narayanan, A. (2021). Brilacidin Demonstrates Inhibition of SARS-CoV-2 in Cell Culture. Viruses, 13.","DOI":"10.3390\/v13020271"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.virol.2020.10.002","article-title":"A natural food preservative peptide nisin can interact with the SARS-CoV-2 spike protein receptor human ACE2","volume":"552","author":"Bhattacharya","year":"2021","journal-title":"Virology"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Liscano, Y., O\u00f1ate-Garz\u00f3n, J., and Ocampo-Ib\u00e1\u00f1ez, I.D. (2020). In Silico Discovery of Antimicrobial Peptides as an Alternative to Control SARS-CoV-2. Molecules, 25.","DOI":"10.3390\/molecules25235535"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1038\/s41392-021-00551-1","article-title":"Antimicrobial peptide DP7 with potential activity against SARS coronavirus infections","volume":"6","author":"Zhang","year":"2021","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"e02123-20","DOI":"10.1128\/mBio.02123-20","article-title":"Antimicrobial peptides: A new frontier in antifungal therapy","volume":"11","author":"Cristy","year":"2020","journal-title":"mBio"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"2169","DOI":"10.3389\/fmicb.2019.02169","article-title":"Bioactive Peptides against Fungal Biofilms","volume":"10","author":"Oshiro","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1007\/s11926-016-0572-1","article-title":"Fungal Infections and New Biologic Therapies","volume":"18","author":"Vallabhaneni","year":"2016","journal-title":"Curr. Rheumatol. Rep."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"S436","DOI":"10.1093\/infdis\/jix210","article-title":"Azole-resistant aspergillosis: Epidemiology, molecular mechanisms, and treatment","volume":"216","author":"Chowdhary","year":"2017","journal-title":"J. Infect. Dis."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1126\/science.aap7999","article-title":"Health and Food Security\u2014TCLocal","volume":"742","author":"Fisher","year":"2018","journal-title":"Science"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1111\/2049-632X.12151","article-title":"Treatment of microbial biofilms in the post-antibiotic era: Prophylactic and therapeutic use of antimicrobial peptides and their design by bioinformatics tools","volume":"70","author":"Maccari","year":"2014","journal-title":"Pathog. Dis."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.biochi.2016.05.013","article-title":"Antifungal peptides: To be or not to be membrane active","volume":"130","author":"Rautenbach","year":"2016","journal-title":"Biochimie"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"105","DOI":"10.3389\/fcimb.2020.00105","article-title":"Antifungal Peptides as Therapeutic Agents","volume":"10","author":"Arbulu","year":"2020","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1517\/13543784.9.2.273","article-title":"De Expert Opinion on Investigational Drugs Antifungal peptides: Potential candidates for the treatment of fungal infections","volume":"9","author":"Lucca","year":"2000","journal-title":"Expert Opin. Investig. Drugs"},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Bondaryk, M., Staniszewska, M., Zieli\u0144ska, P., and Urba\u0144czyk-Lipkowska, Z. (2017). Natural Antimicrobial Peptides as Inspiration for Design of a New Generation Antifungal Compounds. J. Fungi, 3.","DOI":"10.3390\/jof3030046"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"51","DOI":"10.12816\/0029870","article-title":"A review of antifungal peptides: Basis to new era of antifungal drugs","volume":"9","author":"Akkam","year":"2016","journal-title":"Jordan J. Pharm. Sci."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"441","DOI":"10.2217\/fmb-2016-0181","article-title":"Antifungal plant defensins: Increased insight in their mode of action as a basis for their use to combat fungal infections","volume":"12","author":"Cools","year":"2017","journal-title":"Future Microbiol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"2345","DOI":"10.1093\/molbev\/msw106","article-title":"The Defensins Consist of Two Independent, Convergent Protein Superfamilies","volume":"33","author":"Shafee","year":"2016","journal-title":"Mol. Biol. Evol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.semcdb.2018.02.004","article-title":"The evolution, function and mechanisms of action for plant defensins","volume":"88","author":"Parisi","year":"2019","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1033","DOI":"10.1021\/acs.biochem.6b01111","article-title":"Human \u03b1-Defensin 6 Self-Assembly Prevents Adhesion and Suppresses Virulence Traits of Candida albicans","volume":"56","author":"Chairatana","year":"2017","journal-title":"Biochemistry"},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Ballard, E., Yucel, R., Melchers, W.J.G., Brown, A.J.P., Verweij, P.E., and Warris, A. (2020). Antifungal activity of antimicrobial peptides and proteins against Aspergillus fumigatus. J. Fungi, 6.","DOI":"10.3390\/jof6020065"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"6118","DOI":"10.1128\/IAI.00995-06","article-title":"Cryptococcus neoformans cells in biofilms are less susceptible than planktonic cells to antimicrobial molecules produced by the innate immune system","volume":"74","author":"Martinez","year":"2006","journal-title":"Infect. Immun."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0014-5793(95)01050-O","article-title":"Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain","volume":"374","author":"Zanetti","year":"1995","journal-title":"FEBS Lett."},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Ridyard, K.E., and Overhage, J. (2021). The potential of human peptide ll-37 as an antimicrobial and anti-biofilm agent. Antibiotics, 10.","DOI":"10.3390\/antibiotics10060650"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1926","DOI":"10.1128\/MCB.22.6.1926-1935.2002","article-title":"BMAP-28, an Antibiotic Peptide of Innate Immunity, Induces Cell Death through Opening of the Mitochondrial Permeability Transition Pore","volume":"22","author":"Risso","year":"2002","journal-title":"Mol. Cell. Biol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.peptides.2015.07.023","article-title":"Antifungal activity of cathelicidin peptides against planktonic and biofilm cultures of Candida species isolated from vaginal infections","volume":"71","author":"Scarsini","year":"2015","journal-title":"Peptides"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"7472","DOI":"10.1016\/S0021-9258(18)68522-9","article-title":"Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans","volume":"263","author":"Oppenheim","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1016\/j.archoralbio.2009.01.016","article-title":"Sensitivity of Candida albicans Biofilm Cells Grown on Denture Acrylic to Antifungal Proteins and Chlorhexidine","volume":"54","author":"Pusateria","year":"2009","journal-title":"Arch. Oral Biol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1007\/s10482-010-9417-5","article-title":"Susceptibility of Candida biofilms to histatin 5 and fluconazole","volume":"97","author":"Konopka","year":"2010","journal-title":"Antonie van Leeuwenhoek Int. J. Gen. Mol. Microbiol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1007\/978-981-13-3588-4_10","article-title":"Antimicrobial Host Defence Peptides: Immunomodulatory Functions and Translational Prospects","volume":"1117","author":"Hiemstra","year":"2019","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Kang, H.K., Lee, H.H., Seo, C.H., and Park, Y. (2019). Antimicrobial and Immunomodulatory Properties and Applications of Marine-Derived Proteins and Peptides. Mar. Drugs, 17.","DOI":"10.3390\/md17060350"},{"key":"ref_96","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_97","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.3389\/fmicb.2020.01147","article-title":"Fragmentation of Human Neutrophil \u03b1-Defensin 4 to Combat Multidrug Resistant Bacteria","volume":"11","author":"Ehmann","year":"2020","journal-title":"Front. Microbiol."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Guryanova, S.V., and Ovchinnikova, T.V. (2022). Immunomodulatory and Allergenic Properties of Antimicrobial Peptides. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23052499"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"2215","DOI":"10.1007\/s00018-011-0714-6","article-title":"Paneth cell \u03b1-defensins in enteric innate immunity","volume":"68","author":"Ouellette","year":"2011","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Pahar, B., Madonna, S., Das, A., Albanesi, C., and Girolomoni, G. (2020). Immunomodulatory Role of the Antimicrobial LL-37 Peptide in Autoimmune Diseases and Viral Infections. Vaccines, 8.","DOI":"10.3390\/vaccines8030517"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"2072","DOI":"10.3389\/fimmu.2018.03072","article-title":"\u03b2-Defensins: Farming the Microbiome for Homeostasis and Health","volume":"9","author":"Meade","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1159\/000336619","article-title":"\u03b2-Defensins: Multifunctional modulators of infection, inflammation and more?","volume":"4","author":"Semple","year":"2012","journal-title":"J. Innate Immun."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"302","DOI":"10.3389\/fmicb.2018.00302","article-title":"Conceptual Perspectives: Bacterial Antimicrobial Peptide Induction as a Novel Strategy for Symbiosis with the Human Host","volume":"9","author":"Ghosh","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"115","DOI":"10.3389\/fimmu.2015.00115","article-title":"An evolutionary history of defensins: A role for copy number variation in maximizing host innate and adaptive immune responses","volume":"6","author":"Machado","year":"2015","journal-title":"Front. Immunol."},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Candela, M.E., Allsop, D.J.P., Carter, R.N., Semple, F., Kilanowski, F., Webb, S., Taggart, D., Mullan, H.J., McHugh, B.J., and Dockrell, D.H. (2021). Classical macrophage polarisation is limited by human \u03b2-defensin-3 via an autocrine IL-4 dependent process. bioRxiv, Preprint.","DOI":"10.1101\/2021.05.06.442606"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"764","DOI":"10.3389\/fimmu.2020.00764","article-title":"Defensins: A Double-Edged Sword in Host Immunity","volume":"11","author":"Xu","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1038\/s41422-020-0332-7","article-title":"Interaction between microbiota and immunity in health and disease","volume":"30","author":"Zheng","year":"2020","journal-title":"Cell Res."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"107990","DOI":"10.1016\/j.pharmthera.2021.107990","article-title":"Antimicrobial peptides\u2014Unleashing their therapeutic potential using nanotechnology","volume":"232","author":"Gera","year":"2021","journal-title":"Pharmacol. Ther."},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Komatsu, T., Watanabe, K., Hamada, N., Helmerhorst, E., Oppenheim, F., and Lee, M.C. (2021). Il Association between Antimicrobial Peptide Histatin 5 Levels and Prevalence of Candida in Saliva of Patients with Down Syndrome. Antibiotics, 10.","DOI":"10.3390\/antibiotics10050494"},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Sharma, P., Chaudhary, M., Khanna, G., Rishi, P., and Kaur, I.P. (2021). Envisaging Antifungal Potential of Histatin 5: A Physiological Salivary Peptide. J. Fungi, 7.","DOI":"10.3390\/jof7121070"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1002\/med.21435","article-title":"Human Antimicrobial Peptides in Bodily Fluids: Current Knowledge and Therapeutic Perspectives in the Postantibiotic Era","volume":"38","author":"Bastos","year":"2018","journal-title":"Med. Res. Rev."},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Norris, H.L., Kumar, R., Ong, C.Y., Xu, D., and Edgerton, M. (2020). Zinc Binding by Histatin 5 Promotes Fungicidal Membrane Disruption in C. albicans and C. glabrata. J. Fungi, 6.","DOI":"10.3390\/jof6030124"},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"Lee, S.M., Son, K.N., Shah, D., Ali, M., Balasubramaniam, A., Shukla, D., and Aakalu, V.K. (2021). Histatin-1 Attenuates LPS-Induced Inflammatory Signaling in RAW264.7 Macrophages. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22157856"},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"van Harten, R.M., van Woudenbergh, E., van Dijk, A., and Haagsman, H.P. (2018). Cathelicidins: Immunomodulatory Antimicrobials. Vaccines, 6.","DOI":"10.3390\/vaccines6030063"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1799","DOI":"10.4049\/jimmunol.1500021","article-title":"Critical Role of Antimicrobial Peptide Cathelicidin for Controlling Helicobacter pylori Survival and Infection","volume":"196","author":"Zhang","year":"2016","journal-title":"J. Immunol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"610997","DOI":"10.3389\/fmedt.2020.610997","article-title":"Mode-of-Action of Antimicrobial Peptides: Membrane Disruption vs. Intracellular Mechanisms","volume":"2","author":"Benfield","year":"2020","journal-title":"Front. Med. Technol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"2609","DOI":"10.1016\/j.apsb.2021.07.014","article-title":"Membrane-disruptive peptides\/peptidomimetics-based therapeutics: Promising systems to combat bacteria and cancer in the drug-resistant era","volume":"11","author":"Lin","year":"2021","journal-title":"Acta Pharm. Sin. B"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1093\/jac\/dki460","article-title":"Glycosaminoglycans inhibit the antibacterial activity of LL-37 in biological fluids","volume":"57","author":"Sonesson","year":"2006","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"1902","DOI":"10.3389\/fmicb.2020.01902","article-title":"Cathelicidin Host Defense Peptides and Inflammatory Signaling: Striking a Balance","volume":"11","author":"Alford","year":"2020","journal-title":"Front. Microbiol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"149","DOI":"10.3389\/fimmu.2012.00149","article-title":"Multiple immune-modulatory functions of cathelicidin host defense peptides","volume":"3","author":"Choi","year":"2012","journal-title":"Front. Immunol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/415389a","article-title":"Antimicrobial peptides of multicellular organisms","volume":"415","author":"Zasloff","year":"2002","journal-title":"Nature"},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Dash, R., and Bhattacharjya, S. (2021). Thanatin: An Emerging Host Defense Antimicrobial Peptide with Multiple Modes of Action. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22041522"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"100078","DOI":"10.1016\/j.medidd.2020.100078","article-title":"Emerging peptide antibiotics with therapeutic potential","volume":"9","author":"Upert","year":"2021","journal-title":"Med. Drug Discov."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1038\/s41467-022-29234-3","article-title":"A synthetic lipopeptide targeting top-priority multidrug-resistant Gram-negative pathogens","volume":"13","author":"Roberts","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.ijbiomac.2022.07.103","article-title":"In pursuit of next-generation therapeutics: Antimicrobial peptides against superbugs, their sources, mechanism of action, nanotechnology-based delivery, and clinical applications","volume":"218","author":"Thakur","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1007\/s10989-022-10435-9","article-title":"Role of Antimicrobial Peptides in Treatment and Prevention of Mycobacterium Tuberculosis: A Review","volume":"28","author":"Mehta","year":"2022","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"122","DOI":"10.2174\/138920109787048634","article-title":"Advances in peptide pharmaceuticals","volume":"10","author":"Stevenson","year":"2009","journal-title":"Curr. Pharm. Biotechnol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1093\/jac\/dkm357","article-title":"Polymyxin B for the treatment of multidrug-resistant pathogens: A critical review","volume":"60","author":"Zavascki","year":"2007","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1080\/14712598.2017.1315402","article-title":"An overview of antimicrobial peptides and the latest advances in their development","volume":"17","author":"Sierra","year":"2017","journal-title":"Expert Opin. Biol. Ther."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"616979","DOI":"10.3389\/fmicb.2021.616979","article-title":"Review: Lessons Learned From Clinical Trials Using Antimicrobial Peptides (AMPs)","volume":"12","author":"Dijksteel","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1093\/jac\/47.5.709","article-title":"Suppressive effect of Lactobacillus gasseri OLL 2716 (LG21) on Helicobacter pylori infection in humans","volume":"47","author":"Sakamoto","year":"2001","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"31","DOI":"10.4103\/jisp.jisp_326_18","article-title":"The antiplaque efficacy of lantibiotic Nisin extract mouthrinse","volume":"23","author":"Mitra","year":"2019","journal-title":"J. Indian Soc. Periodontol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1080\/07420528.2020.1782419","article-title":"Crosstalk between circulating microRNAs and chronotypical features in subjects with metabolic syndrome","volume":"37","author":"Assmann","year":"2020","journal-title":"Chronobiol. Int."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"174","DOI":"10.3389\/fcimb.2019.00174","article-title":"Characterization of the in vitro, ex vivo, and in vivo Efficacy of the Antimicrobial Peptide DPK-060 Used for Topical Treatment","volume":"9","author":"Ringstad","year":"2019","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"van der Velden, W.J.F.M., van Iersel, T.M.P., Blijlevens, N.M.A., and Donnelly, J.P. (2009). Safety and tolerability of the antimicrobial peptide human lactoferrin 1-11 (hLF1-11). BMC Med., 7.","DOI":"10.1186\/1741-7015-7-44"},{"key":"ref_136","first-page":"620","article-title":"Antimicrobial Peptides under Clinical Trials","volume":"17","author":"Dawgul","year":"2017","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1080\/14787210.2018.1441024","article-title":"Murepavadin: A new antibiotic class in the pipeline","volume":"16","author":"Dale","year":"2018","journal-title":"Expert Rev. Anti. Infect. Ther."},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Wiig, M.E., Dahlin, L.B., Frid\u00e9n, J., Hagberg, L., Larsen, S.E., Wiklund, K., and Mahlapuu, M. (2014). PXL01 in sodium hyaluronate for improvement of hand recovery after flexor tendon repair surgery: Randomized controlled trial. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0110735"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1111\/wrr.12211","article-title":"Treatment with LL-37 is safe and effective in enhancing healing of hard-to-heal venous leg ulcers: A randomized, placebo-controlled clinical trial","volume":"22","author":"Mahlapuu","year":"2014","journal-title":"Wound Repair Regen."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1111\/wrr.12977","article-title":"Evaluation of LL-37 in healing of hard-to-heal venous leg ulcers: A multicentric prospective randomized placebo-controlled clinical trial","volume":"29","author":"Mahlapuu","year":"2021","journal-title":"Wound Repair Regen."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1038\/nri.2016.29","article-title":"The immunology of host defence peptides: Beyond antimicrobial activity","volume":"16","author":"Hancock","year":"2016","journal-title":"Nat. Rev. Immunol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"944147","DOI":"10.3389\/fphar.2022.944147","article-title":"Renovation as innovation: Repurposing human antibacterial peptide LL-37 for cancer therapy","volume":"13","author":"Lu","year":"2022","journal-title":"Front. Pharmacol."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Tokajuk, J., Deptu\u0142a, P., Piktel, E., Daniluk, T., Chmielewska, S., Wollny, T., Wolak, P., Fiedoruk, K., and Bucki, R. (2022). Cathelicidin LL-37 in Health and Diseases of the Oral Cavity. Biomedicines, 10.","DOI":"10.3390\/biomedicines10051086"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1177\/0022034519877386","article-title":"Precision Reengineering of the Oral Microbiome for Caries Management","volume":"30","author":"Baker","year":"2019","journal-title":"Adv. Dent. Res."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1111\/j.1600-0714.2011.01094.x","article-title":"The antimicrobial effect of Iseganan HCl oral solution in patients receiving stomatotoxic chemotherapy: Analysis from a multicenter, double-blind, placebo-controlled, randomized, phase III clinical trial","volume":"41","author":"Elad","year":"2012","journal-title":"J. Oral Pathol. Med."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.oraloncology.2019.05.013","article-title":"Oral mucositis in head and neck cancer: Evidence-based management and review of clinical trial data","volume":"95","author":"Blakaj","year":"2019","journal-title":"Oral Oncol."},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"Zhao, C., Yan, S., Song, Y., and Xia, X. (2022). Roles of Antimicrobial Peptides in Gynecological Cancers. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms231710104"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1096\/fj.04-3284com","article-title":"Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly up-regulated in myeloid cells by 1,25-dihydroxyvitamin D3","volume":"19","author":"Gombart","year":"2005","journal-title":"FASEB J."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"2060","DOI":"10.4049\/jimmunol.179.4.2060","article-title":"Cutting edge: Vitamin D-mediated human antimicrobial activity against Mycobacterium tuberculosis is dependent on the induction of cathelicidin","volume":"179","author":"Liu","year":"2007","journal-title":"J. Immunol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"888168","DOI":"10.3389\/fpubh.2022.888168","article-title":"Vitamin D: A Potential Mitigation Tool for the Endemic Stage of the COVID-19 Pandemic?","volume":"10","author":"Savelkoul","year":"2022","journal-title":"Front. Public Health"},{"key":"ref_151","doi-asserted-by":"crossref","unstructured":"Dixon, B.M., Barker, T., McKinnon, T., Cuomo, J., Frei, B., Borregaard, N., and Gombart, A.F. (2012). Positive correlation between circulating cathelicidin antimicrobial peptide (hCAP18\/LL-37) and 25-hydroxyvitamin D levels in healthy adults. BMC Res. Notes, 5.","DOI":"10.1186\/1756-0500-5-575"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.nut.2017.02.002","article-title":"Impact of high-dose vitamin D 3 on plasma free 25-hydroxyvitamin D concentrations and antimicrobial peptides in critically ill mechanically ventilated adults","volume":"38","author":"Han","year":"2017","journal-title":"Nutrition"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"bbac343","DOI":"10.1093\/bib\/bbac343","article-title":"Benchmarks in antimicrobial peptide prediction are biased due to the selection of negative data","volume":"23","author":"Sidorczuk","year":"2022","journal-title":"Brief. Bioinform."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.drudis.2009.10.009","article-title":"Synthetic therapeutic peptides: Science and market","volume":"15","author":"Vlieghe","year":"2010","journal-title":"Drug Discov. Today"},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Makowski, M., Silva, \u00cd.C., Do Amaral, C.P., Gon\u00e7alves, S., and Santos, N.C. (2019). Advances in lipid and metal nanoparticles for antimicrobial peptide delivery. Pharmaceutics, 11.","DOI":"10.3390\/pharmaceutics11110588"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"128","DOI":"10.3389\/fcimb.2019.00128","article-title":"Application of antimicrobial peptides of the innate immune system in combination with conventional antibiotics\u2014A novel way to combat antibiotic resistance?","volume":"9","author":"Zharkova","year":"2019","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"105827","DOI":"10.1016\/j.ijantimicag.2019.10.008","article-title":"Efficacy of newly generated short antimicrobial cationic lipopeptides against methicillin-resistant Staphylococcus aureus (MRSA)","volume":"55","author":"Greber","year":"2020","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_158","doi-asserted-by":"crossref","unstructured":"Lesiuk, M., Paduszy\u0144ska, M., and Greber, K.E. (2022). Synthetic Antimicrobial Immunomodulatory Peptides: Ongoing Studies and Clinical Trials. Antibiotics, 11.","DOI":"10.3390\/antibiotics11081062"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1002\/bip.22250","article-title":"Peptide design for antimicrobial and immunomodulatory applications","volume":"100","author":"Haney","year":"2013","journal-title":"Biopolymers"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1038\/nchembio.1393","article-title":"Immune modulation by multifaceted cationic host defense (antimicrobial) peptides","volume":"9","author":"Hilchie","year":"2013","journal-title":"Nat. Chem. Biol."},{"key":"ref_161","doi-asserted-by":"crossref","unstructured":"Drayton, M., Deisinger, J.P., Ludwig, K.C., Raheem, N., M\u00fcller, A., Schneider, T., and Straus, S.K. (2021). Host Defense Peptides: Dual Antimicrobial and Immunomodulatory Action. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222011172"}],"container-title":["Antibiotics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2079-6382\/11\/10\/1417\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T00:55:03Z","timestamp":1760144103000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2079-6382\/11\/10\/1417"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,10,16]]},"references-count":161,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2022,10]]}},"alternative-id":["antibiotics11101417"],"URL":"https:\/\/doi.org\/10.3390\/antibiotics11101417","relation":{},"ISSN":["2079-6382"],"issn-type":[{"value":"2079-6382","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,10,16]]}}}