{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T04:47:35Z","timestamp":1787028455457,"version":"build-2736575974"},"reference-count":157,"publisher":"MDPI AG","issue":"15","license":[{"start":{"date-parts":[[2021,7,25]],"date-time":"2021-07-25T00:00:00Z","timestamp":1627171200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Universidad Santiago de Cali","award":["934-621121-2367"],"award-info":[{"award-number":["934-621121-2367"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The emergence of bacteria resistant to conventional antibiotics is of great concern in modern medicine because it renders ineffectiveness of the current empirical antibiotic therapies. Infections caused by vancomycin-resistant Staphylococcus aureus (VRSA) and vancomycin-intermediate S. aureus (VISA) strains represent a serious threat to global health due to their considerable morbidity and mortality rates. Therefore, there is an urgent need of research and development of new antimicrobial alternatives against these bacteria. In this context, the use of antimicrobial peptides (AMPs) is considered a promising alternative therapeutic strategy to control resistant strains. Therefore, a wide number of natural, artificial, and synthetic AMPs have been evaluated against VRSA and VISA strains, with great potential for clinical application. In this regard, we aimed to present a comprehensive and systematic review of research findings on AMPs that have shown antibacterial activity against vancomycin-resistant and vancomycin-intermediate resistant strains and clinical isolates of S. aureus, discussing their classification and origin, physicochemical and structural characteristics, and possible action mechanisms. This is the first review that includes all peptides that have shown antibacterial activity against VRSA and VISA strains exclusively.<\/jats:p>","DOI":"10.3390\/ijms22157927","type":"journal-article","created":{"date-parts":[[2021,7,25]],"date-time":"2021-07-25T22:06:21Z","timestamp":1627250781000},"page":"7927","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":33,"title":["Antimicrobial Peptides with Antibacterial Activity against Vancomycin-Resistant Staphylococcus aureus Strains: Classification, Structures, and Mechanisms of Action"],"prefix":"10.3390","volume":"22","author":[{"given":"Isabella","family":"Hern\u00e1ndez-Aristiz\u00e1bal","sequence":"first","affiliation":[{"name":"Research Group of Microbiology, Industry and Environment, Faculty of Basic Sciences, Universidad Santiago de Cali, Cali 760035, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9833-3537","authenticated-orcid":false,"given":"Iv\u00e1n Dar\u00edo","family":"Ocampo-Ib\u00e1\u00f1ez","sequence":"additional","affiliation":[{"name":"Research Group of Microbiology, Industry and Environment, Faculty of Basic Sciences, Universidad Santiago de Cali, Cali 760035, Colombia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,7,25]]},"reference":[{"key":"ref_1","first-page":"277","article-title":"The Antibiotic Resistance: Part 1: Causes and threats","volume":"40","author":"Ventola","year":"2015","journal-title":"Pharm. Ther."},{"key":"ref_2","unstructured":"WHO (2017). Global Antimicrobial Resistance Surveillance System (GLASS) Report, World Health Organization."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1016\/j.cmi.2015.12.002","article-title":"The negative impact of antibiotic resistance","volume":"22","author":"Friedman","year":"2016","journal-title":"Clin. Microbiol. Infect"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"S48","DOI":"10.1093\/cid\/civ523","article-title":"Evolving Resistance among Gram-positive Pathogens","volume":"61","author":"Munita","year":"2015","journal-title":"Clin. Infect Dis."},{"key":"ref_5","unstructured":"World Health Organization (2021, May 28). Lack of New Antibiotics Threatens Global Efforts to Contain Drug-Resistant Infections. Available online: https:\/\/www.who.int\/news\/item\/17-01-2020-lack-of-new-antibiotics-threatens-global-efforts-to-contain-drug-resistant-infections."},{"key":"ref_6","first-page":"179","article-title":"Gram-positive bacterial resistance: A challenge for the next millennium","volume":"44","author":"Bassetti","year":"2002","journal-title":"Panminerva Med."},{"key":"ref_7","unstructured":"World Health Organization (2021, May 25). WHO Publishes List of Bacteria for Which New Antibiotics Are Urgently Needed. Available online: https:\/\/www.who.int\/news-room\/detail\/27-02-2017-who-publishes-list-of-bacteria-for-which-new-antibiotics-are-urgently-needed."},{"key":"ref_8","unstructured":"WHO (2017). Global Priority List of Antibiotic-Resistant Bacteria to Guide Research, Discovery, and Development of New Antibiotics, World Health Organization."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1038\/s41579-018-0147-4","article-title":"Methicillin-resistant Staphylococcus aureus: An overview of basic and clinical research","volume":"17","author":"Turner","year":"2019","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1038\/nrmicro2200","article-title":"Waves of resistance: Staphylococcus aureus in the antibiotic era","volume":"7","author":"Chambers","year":"2009","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"18033","DOI":"10.1038\/nrdp.2018.33","article-title":"Methicillin-resistant Staphylococcus aureus","volume":"4","author":"Lee","year":"2018","journal-title":"Nat. Rev. Dis. Prim."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Jubeh, B., Breijyeh, Z., and Karaman, R. (2020). Resistance of gram-positive bacteria to current antibacterial agents and overcoming approaches. Molecules, 25.","DOI":"10.3390\/molecules25122888"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.1021\/bi5000564","article-title":"Mechanism of quinolone action and resistance","volume":"53","author":"Aldred","year":"2014","journal-title":"Biochemistry"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Krause, K.M., Serio, A.W., Kane, T.R., and Connolly, L.E. (2020). Aminoglycosides: An overview. Cold Spring Harb. Perspect Med., 6.","DOI":"10.1101\/cshperspect.a027029"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"184","DOI":"10.3904\/kjim.2016.351","article-title":"Clinical and microbiological factors associated with early patient mortality from methicillin- resistant Staphylococcus aureus bacteremia","volume":"34","author":"Kim","year":"2019","journal-title":"Korean J. Intern. Med."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-020-69058-z","article-title":"Global prevalence and distribution of vancomycin resistant, vancomycin intermediate and heterogeneously vancomycin intermediate Staphylococcus aureus clinical isolates: A systematic review and meta-analysis","volume":"10","author":"Shariati","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"781679","DOI":"10.1155\/2012\/781679","article-title":"Glycopeptide resistance in gram-positive Cocci: A review","volume":"2012","author":"Sujatha","year":"2012","journal-title":"Interdiscip Perspect Infect Dis."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1093\/cid\/cir920","article-title":"Oritavancin: Mechanism of action","volume":"54","author":"Zhanel","year":"2012","journal-title":"Clin. Infect Dis."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1038\/s41586-020-1990-9","article-title":"Evolution-guided discovery of antibiotics that inhibit peptidoglycan remodelling","volume":"578","author":"Culp","year":"2020","journal-title":"Nature"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"111","DOI":"10.3389\/fcell.2016.00111","article-title":"Antimicrobial activity of cationic antimicrobial peptides against gram-positives: Current progress made in understanding the mode of action and the response of bacteria","volume":"4","author":"Omardien","year":"2016","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Yu, G., Baeder, D.Y., Regoes, R.R., and Rolff, J. (2018). Predicting drug resistance evolution: Insights from antimicrobial peptides and antibiotics. Proc. Biol. Sci., 285.","DOI":"10.1098\/rspb.2017.2687"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Wang, S., Zeng, X., Yang, Q., and Qiao, S. (2016). Antimicrobial peptides as potential alternatives to antibiotics in food animal industry. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17050603"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.it.2008.12.003","article-title":"AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense","volume":"30","author":"Lai","year":"2009","journal-title":"Trends Immunol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1","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_25","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1016\/j.peptides.2003.08.023","article-title":"The relationship between peptide structure and antibacterial activity","volume":"24","author":"Powers","year":"2003","journal-title":"Peptides"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2161","DOI":"10.1007\/s00018-011-0710-x","article-title":"Multifunctional cationic host defence peptides and their clinical applications","volume":"68","author":"Yeung","year":"2011","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1006\/bbrc.1998.8159","article-title":"Mechanism of Action of the Antimicrobial Peptide Buforin II: Buforin II Kills Microorganisms by Penetrating the Cell Membrane and Inhibiting Cellular Functions","volume":"244","author":"Park","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1021\/acsinfecdis.8b00204","article-title":"Structure-Activity Relationships of the Bacteriocin Bactofencin A and Its Interaction with the Bacterial Membrane","volume":"5","author":"Fliss","year":"2019","journal-title":"ACS Infect Dis."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"5220","DOI":"10.1128\/AAC.00369-11","article-title":"Ctriporin, a new anti-methicillin-resistant Staphylococcus aureus peptide from the venom of the scorpion Chaerilus tricostatus","volume":"55","author":"Fan","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1179\/2047773215Y.0000000030","article-title":"Antimicrobial resistance: A global multifaceted phenomenon","volume":"109","author":"Prestinaci","year":"2015","journal-title":"Pathog. Glob. Health"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"3040","DOI":"10.1128\/AAC.47.10.3040-3045.2003","article-title":"Staphylococcus aureus with Heterogeneous Resistance to Vancomycin: Epidemiology, Clinical Significance, and Critical Assessment of Diagnostic Methods","volume":"47","author":"Liu","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"15359","DOI":"10.1038\/s41598-018-33593-7","article-title":"Genomics of experimental adaptation of Staphylococcus aureus to a natural combination of insect antimicrobial peptides","volume":"8","author":"Makarova","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"103","DOI":"10.3389\/fmicb.2020.00103","article-title":"Resistance Evolution Against Antimicrobial Peptides in Staphylococcus aureus Alters Pharmacodynamics Beyond the MIC","volume":"11","author":"Yu","year":"2020","journal-title":"Front. Microbiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1038\/ja.2016.101","article-title":"Activity of tick antimicrobial peptide from Ixodes persulcatus (persulcatusin) against cell membranes of drug-resistant Staphylococcus aureus","volume":"70","author":"Miyoshi","year":"2017","journal-title":"J. Antibiot. (Tokyo)"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.2147\/IDR.S160975","article-title":"Novel vancomycin\u2013peptide conjugate as potent antibacterial agent against vancomycin-resistant Staphylococcus aureus","volume":"11","author":"Jelinkova","year":"2018","journal-title":"Infect Drug Resist."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"4478","DOI":"10.1128\/AAC.00194-12","article-title":"In Vitro activities of LTX-109, a synthetic antimicrobial peptide, against methicillin-resistant, vancomycin-intermediate, vancomycin-resistant, daptomycin-nonsusceptible, and linezolid-nonsusceptible Staphylococcus aureus","volume":"56","author":"Saravolatz","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep29707","article-title":"Evaluation of short synthetic antimicrobial peptides for treatment of drug-resistant and intracellular Staphylococcus aureus","volume":"6","author":"Mohamed","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1007\/s12223-016-0479-2","article-title":"Antimicrobial peptide isolated from Bacillus amyloliquefaciens K14 revitalizes its use in combinatorial drug therapy","volume":"62","author":"Regmi","year":"2017","journal-title":"Folia Microbiol. (Praha)"},{"key":"ref_39","first-page":"45","article-title":"Antimicrobial peptide from Bacillus subtilis CSB138: Characterization, killing kinetics, and synergistic potency","volume":"20","author":"Regmi","year":"2017","journal-title":"Int. Microbiol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2235","DOI":"10.1016\/j.bmc.2016.03.053","article-title":"Short cationic lipopeptides as effective antibacterial agents: Design, physicochemical properties and biological evaluation","volume":"24","author":"Azmi","year":"2016","journal-title":"Bioorganic Med. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1038\/s41429-018-0090-7","article-title":"Evaluation of LL-37 antimicrobial peptide derivatives alone and in combination with vancomycin against S. aureus","volume":"71","author":"Shurko","year":"2018","journal-title":"J. Antibiot."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/j.diagmicrobio.2007.11.004","article-title":"In Vitro activity of omiganan pentahydrochloride tested against vancomycin-tolerant, -intermediate, and -resistant Staphylococcus aureus","volume":"60","author":"Fritsche","year":"2008","journal-title":"Diagn. Microbiol. Infect Dis."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Wu, C., Hsueh, J., Yip, B., Chih, Y., Peng, K., and Cheng, J. (2020). Antimicrobial Peptides Display Strong Synergy with Vancomycin Against Vancomycin-Resistant. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21134578"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.ijantimicag.2008.07.028","article-title":"Pharmacodynamic activity of the lantibiotic MU1140","volume":"33","author":"Ghobrial","year":"2009","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.ijantimicag.2012.03.019","article-title":"A novel thermotolerant and acidotolerant peptide produced by a Bacillus strain newly isolated from a fermented food (kimchi) shows activity against multidrug-resistant bacteria","volume":"40","author":"Choi","year":"2012","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Wang, B., Yao, Y., Wei, P., Song, C., Wan, S., Yang, S., Zhu, G.M., and Liu, H.M. (2020). Housefly Phormicin inhibits Staphylococcus aureus and MRSA by disrupting biofilm formation and altering gene expression In Vitro and In Vivo. Int. J. Biol. Macromol.","DOI":"10.1016\/j.ijbiomac.2020.11.096"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"4113","DOI":"10.1128\/AAC.02578-14","article-title":"Targeting methicillin-resistant Staphylococcus aureus with short salt-resistant synthetic peptides","volume":"58","author":"Mohamed","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1002\/cbic.202000716","article-title":"Antimicrobial and Anticancer Properties of Synthetic Peptides Derived from the Wasp Parachartergus fraternus","volume":"22","author":"Muller","year":"2021","journal-title":"Chem. Biol. Chem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2600","DOI":"10.1016\/j.peptides.2006.05.004","article-title":"Experimental study on the efficacy of combination of \u03b1-helical antimicrobial peptides and vancomycin against Staphylococcus aureus with intermediate resistance to glycopeptides","volume":"27","author":"Cirioni","year":"2006","journal-title":"Peptides"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"105592","DOI":"10.1016\/j.ejps.2020.105592","article-title":"In-depth characterization of antibacterial activity of melittin against Staphylococcus aureus and use in a model of non-surgical MRSA-infected skin wounds","volume":"156","author":"Lima","year":"2021","journal-title":"Eur. J. Pharm. Sci."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fcell.2016.00086","article-title":"Towards profiles of resistance development and toxicity for the small cationic hexapeptide RWRWRW-NH 2","volume":"4","author":"Wenzel","year":"2016","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.bbrc.2010.07.024","article-title":"Characterization and structure identification of an antimicrobial peptide, hominicin, produced by Staphylococcus hominis MBBL 2-9","volume":"399","author":"Kim","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1093\/jac\/dkp221","article-title":"A comparison of the activities of lacticin 3147 and nisin against drug-resistant Staphylococcus aureus and Enterococcus species","volume":"64","author":"Piper","year":"2009","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.toxicon.2016.03.014","article-title":"Characterisation of three alpha-helical antimicrobial peptides from the venom of Scorpio maurus palmatus","volume":"117","author":"Harrison","year":"2016","journal-title":"Toxicon"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/1471-2180-8-186","article-title":"The lantibiotic mersacidin is a strong inducer of the cell wall stress response of Staphylococcus aureus","volume":"8","author":"Sass","year":"2008","journal-title":"BMC Microbiol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.peptides.2018.05.011","article-title":"Antibacterial, Antifungal, Anticancer Activities and Structural Bioinformatics Analysis of Six Naturally Occurring Temporins","volume":"1","author":"Mishra","year":"2018","journal-title":"Peptides"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1002\/cmdc.201200016","article-title":"Effects of cyclic lipodepsipeptide structural modulation on stability, antibacterial activity and human cell toxicity","volume":"7","author":"Bionda","year":"2012","journal-title":"Chem. Med. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1038\/nature18634","article-title":"Human commensals producing a novel antibiotic impair pathogen colonization","volume":"535","author":"Zipperer","year":"2016","journal-title":"Nature"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"59758","DOI":"10.1039\/C5RA07896B","article-title":"Small lipopeptides possess anti-biofilm capability comparable to daptomycin and vancomycin","volume":"5","author":"Mishra","year":"2015","journal-title":"RSC Adv."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1969","DOI":"10.1110\/ps.072966007","article-title":"Structure-activity study of the antibacterial peptide fallaxin","volume":"16","author":"Nielsen","year":"2007","journal-title":"Protein Sci."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Garoy, E.Y., Gebreab, Y.B., Achila, O.O., Tekeste, D.G., Kesete, R., Ghirmay, R., Kiflay, R., and Tesfu, T. (2019). Methicillin-Resistant Staphylococcus aureus (MRSA): Prevalence and Antimicrobial Sensitivity Pattern among Patients\u2014A Multicenter Study in Asmara, Eritrea. Can. J. Infect Dis. Med. Microbiol., 2019.","DOI":"10.1155\/2019\/8321834"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/mBio.01105-19","article-title":"Evolution and global transmission of a multidrug-resistant, community-associated methicillin-resistant staphylococcus aureus lineage from the Indian subcontinent","volume":"10","author":"Steinig","year":"2019","journal-title":"MBio"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.jgar.2020.02.025","article-title":"A synergistic association between adhesion-related genes and multidrug resistance patterns of Staphylococcus aureus isolates from different patients and healthy individuals","volume":"22","author":"Parastan","year":"2020","journal-title":"J. Glob. Antimicrob. Resist."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/j.ijantimicag.2013.11.005","article-title":"Activity of ceftobiprole against methicillin-resistant Staphylococcus aureus strains with reduced susceptibility to daptomycin, linezolid or vancomycin, and strains with defined SCCmec types","volume":"43","author":"Farrell","year":"2014","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Shekarabi, M., Hajikhani, B., Salimi Chirani, A., Fazeli, M., and Goudarzi, M. (2017). Molecular characterization of vancomycin-resistant Staphylococcus aureus strains isolated from clinical samples: A three year study in Tehran, Iran. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0183607"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-017-06329-2","article-title":"Role of SCCmec type in resistance to the synergistic activity of oxacillin and cefoxitin in MRSA","volume":"7","author":"Reichmann","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1128\/AAC.44.6.1549-1555.2000","article-title":"A new class of genetic element, staphylococcus cassette chromosome mec, encodes methicillin resistance in Staphylococcus aureus","volume":"44","author":"Katayama","year":"2000","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1136\/jcp.14.4.385","article-title":"Methicillin-resistant staphylococci","volume":"14","author":"BARBER","year":"1961","journal-title":"J. Clin. Pathol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/j.jiac.2014.08.001","article-title":"Multi-drug-resistant Staphylococcus aureus and future chemotherapy","volume":"20","author":"Hiramatsu","year":"2014","journal-title":"J. Infect Chemother"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1128\/CMR.10.4.781","article-title":"Methicillin resistance in staphylococci: Molecular and biochemical basis and clinical implications","volume":"10","author":"Chambers","year":"1997","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.1128\/AAC.45.5.1323-1336.2001","article-title":"Structural comparison of three types of staphylococcal cassette chromosome mec integrated in the chromosome in methicillin-resistant Staphylococcus aureus","volume":"45","author":"Ito","year":"2001","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"2723","DOI":"10.3389\/fmicb.2018.02723","article-title":"Factors contributing to the evolution of Meca-mediated \u03b2-lactam resistance in staphylococci: Update and new insights from whole genome sequencing (WGS)","volume":"9","author":"Miragaia","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"575","DOI":"10.4067\/S0716-10182002000300012","article-title":"Staphylococcus aureus resistente a vancomicina","volume":"19","author":"Mella","year":"2002","journal-title":"Rev. Chil. Infectol."},{"key":"ref_74","unstructured":"CLSI (2017). Performance Standards for Antimicrobial Susceptibility Testing, Clinical and Laboratory Standards Institute. Twenty-Seventh Informational Supplement, CLSI Document M100-S27."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.jare.2019.10.005","article-title":"Vancomycin resistant Staphylococcus aureus infections: A review of case updating and clinical features","volume":"21","author":"Cong","year":"2020","journal-title":"J. Adv. Res."},{"key":"ref_76","first-page":"269","article-title":"Vancomycin resistance in Staphylococcus aureus","volume":"90","author":"McGuinness","year":"2017","journal-title":"Yale J. Biol. Med."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"275","DOI":"10.4103\/0974-777X.68535","article-title":"Methicillin and vancomycin resistant S. aureus in hospitalized patients","volume":"2","author":"Loomba","year":"2010","journal-title":"J. Glob. Infect Dis."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1128\/CMR.00042-09","article-title":"Reduced vancomycin susceptibility in Staphylococcus aureus, including vancomycin-intermediate and heterogeneous vancomycin-intermediate strains: Resistance mechanisms, laboratory detection, and clinical implications","volume":"23","author":"Howden","year":"2010","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1128\/IAI.01030-15","article-title":"The GraS sensor in Staphylococcus aureus mediates resistance to host defense peptides differing in mechanisms of action","volume":"84","author":"Chaili","year":"2016","journal-title":"Infect Immun."},{"key":"ref_80","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_81","doi-asserted-by":"crossref","first-page":"939","DOI":"10.2147\/DDDT.S107195","article-title":"Synergistic effects of antimicrobial peptide DP7 combined with antibiotics against multidrug-resistant bacteria","volume":"11","author":"Wu","year":"2017","journal-title":"Drug Des. Devel. Ther."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.3390\/ph6081055","article-title":"Characterization of antimicrobial peptides toward the development of novel antibiotics","volume":"6","author":"Aoki","year":"2013","journal-title":"Pharmaceuticals"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1093\/icb\/43.2.300","article-title":"The Role of Antimicrobial Peptides in Innate Immunity","volume":"43","author":"Ganz","year":"2003","journal-title":"Integr. Comp. Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/j.jsps.2015.02.015","article-title":"Oral antimicrobial peptides: Types and role in the oral cavity","volume":"24","author":"Khurshid","year":"2016","journal-title":"Saudi Pharm. J."},{"key":"ref_85","first-page":"1","article-title":"Antimicrobial activity and mechanism of action of a novel peptide present in the ecdysis process of centipede Scolopendra subspinipes subspinipes","volume":"9","author":"Alves","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"2664","DOI":"10.1182\/blood.V96.8.2664","article-title":"Antimicrobial proteins and peptides of blood: Templates for novel antimicrobial agents","volume":"96","author":"Levy","year":"2000","journal-title":"Blood"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1847","DOI":"10.1007\/s11274-010-0643-9","article-title":"Antimicrobial peptides derived from different animals: Comparative studies of antimicrobial properties, cytotoxicity and mechanism of action","volume":"27","author":"Han","year":"2011","journal-title":"World J. Microbiol. Biotechnol."},{"key":"ref_88","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_89","doi-asserted-by":"crossref","unstructured":"Brady, D., Grapputo, A., Romoli, O., and Sandrelli, F. (2019). Insect cecropins, antimicrobial peptides with potential therapeutic applications. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20235862"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"6483","DOI":"10.3892\/mmr.2015.4275","article-title":"Melittin, a honeybee venom-derived antimicrobial peptide, may target methicillin-resistant Staphylococcus aureus","volume":"12","author":"Choi","year":"2015","journal-title":"Mol. Med. Rep."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1179\/1973947812Y.0000000007","article-title":"In vitro activities of antimicrobial cationic peptides; melittin and nisin, alone or in combination with antibiotics against Gram-positive bacteria","volume":"24","author":"Dosler","year":"2012","journal-title":"J. Chemother"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1007\/s00726-018-2596-5","article-title":"Action mechanism of melittin-derived antimicrobial peptides, MDP1 and MDP2, de novo designed against multidrug resistant bacteria","volume":"50","author":"Akbari","year":"2018","journal-title":"Amino Acids"},{"key":"ref_93","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_94","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.toxicon.2004.04.009","article-title":"Structural and biological characterization of two novel peptides from the venom of the neotropical social wasp Agelaia pallipes pallipes","volume":"44","author":"Mendes","year":"2004","journal-title":"Toxicon"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"2851","DOI":"10.3390\/toxins2122851","article-title":"Spider-venom peptides as therapeutics","volume":"2","author":"Saez","year":"2010","journal-title":"Toxins"},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Estrada-Pe\u00f1a, A., Cabezas-Cruz, A., and Obreg\u00f3n, D. (2020). Resistance of tick gut microbiome to anti-tick vaccines, pathogen infection and antimicrobial peptides. Pathogens, 9.","DOI":"10.3390\/pathogens9040309"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1111\/j.1365-2583.2009.00897.x","article-title":"Identification and characterization of antimicrobial peptide, defensin, in the taiga tick, ixodes persulcatus","volume":"18","author":"Saito","year":"2009","journal-title":"Insect Mol. Biol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"5757","DOI":"10.1529\/biophysj.108.133488","article-title":"Magainin 2 in action: Distinct modes of membrane permeabilization in living bacterial and mammalian cells","volume":"95","author":"Imura","year":"2008","journal-title":"Biophys. J."},{"key":"ref_99","first-page":"452567","article-title":"Dermaseptins and magainins: Antimicrobial peptides from frogs\u2019 skin-new sources for a promising spermicides microbicides-a mini review","volume":"2009","author":"Hani","year":"2009","journal-title":"J. Biomed. Biotechnol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1089\/sur.2019.266","article-title":"Temporins: An Approach of Potential Pharmaceutic Candidates","volume":"21","author":"Romero","year":"2020","journal-title":"Surg. Infect"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1007\/BF02930945","article-title":"Mammalian antibiotic peptides","volume":"48","author":"Sigler","year":"2003","journal-title":"Folia Microbiol. (Praha)"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1408","DOI":"10.1016\/j.bbamem.2006.03.030","article-title":"LL-37, the only human member of the cathelicidin family of antimicrobial peptides","volume":"1758","author":"Sudheendra","year":"2006","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_103","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_104","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12866-019-1416-8","article-title":"Cationic antimicrobial peptides: Alternatives and\/or adjuvants to antibiotics active against methicillin-resistant Staphylococcus aureus and multidrug-resistant Pseudomonas aeruginosa","volume":"19","author":"Geitani","year":"2019","journal-title":"BMC Microbiol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1038\/nrmicro2259","article-title":"Bacterial competition: Surviving and thriving in the microbial jungle","volume":"8","author":"Hibbing","year":"2010","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_106","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-a novel way to combat antibiotic resistance?","volume":"9","author":"Zharkova","year":"2019","journal-title":"Front. Cell. Infect Microbiol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.ifset.2018.06.008","article-title":"Nisin and other antimicrobial peptides: Production, mechanisms of action, and application in active food packaging","volume":"48","author":"Santos","year":"2018","journal-title":"Innov. Food Sci. Emerg. Technol."},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Simons, A., Alhanout, K., and Duval, R.E. (2020). Bacteriocins, antimicrobial peptides from bacterial origin: Overview of their biology and their impact against multidrug-resistant bacteria. Microorganisms, 8.","DOI":"10.3390\/microorganisms8050639"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1016\/j.bcp.2006.01.012","article-title":"Investigation of the cytotoxicity of eukaryotic and prokaryotic antimicrobial peptides in intestinal epithelial cells In Vitro","volume":"71","author":"Maher","year":"2006","journal-title":"Biochem. Pharmacol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fmicb.2018.00415","article-title":"Mutacin 1140 lantibiotic variants are efficacious against Clostridium difficile infection","volume":"9","author":"Kers","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"e01626-18","DOI":"10.1128\/AAC.01626-18","article-title":"Efficacious Analogs of the Lantibiotic Mutacin 1140 against a Systemic Methicillin-Resistant Staphylococcus aureus Infection","volume":"62","author":"Geng","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1093\/jac\/dkh387","article-title":"Mersacidin eradicates methicillin-resistant Staphylococcus aureus (MRSA) in a mouse rhinitis model","volume":"54","author":"Kruszewska","year":"2004","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fmicb.2016.01493","article-title":"Kimchi and other widely consumed traditional fermented foods of Korea: A review","volume":"7","author":"Patra","year":"2016","journal-title":"Front. Microbiol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"3825","DOI":"10.1111\/1541-4337.12651","article-title":"Bioactive peptides from food fermentation: A comprehensive review of their sources, bioactivities, applications, and future development","volume":"19","author":"Chai","year":"2020","journal-title":"Compr. Rev. Food Sci. Food Saf."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.mib.2019.03.004","article-title":"Toward computer-made artificial antibiotics","volume":"51","author":"Torres","year":"2019","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_116","first-page":"96","article-title":"Properties and design of antimicrobial peptides as potential tools against pathogens and malignant cells","volume":"5","year":"2016","journal-title":"Investig. Discapac."},{"key":"ref_117","unstructured":"Lytix Bipharma (2021, May 26). LTX-109\u2014A High Value Game Changer in Diabetic Foot Infections. Successful Proof of Concept for Topical Antimicrobial Drug Lytixar (LTX-109) . Available online: https:\/\/www.lytixbiopharma.com\/news\/152\/130\/Successful-Proof-of-Concept-for-topical-antimicrobial-drug-Lytixar-LTX-109.html."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.ijantimicag.2009.05.003","article-title":"Antimicrobial and antifungal activities of a novel cationic antimicrobial peptide, omiganan, in experimental skin colonisation models","volume":"34","author":"Rubinchik","year":"2009","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"3112","DOI":"10.1128\/AAC.48.8.3112-3118.2004","article-title":"Omiganan pentahydrochloride (MBI 226), a topical 12-amino-acid cationic peptide: Spectrum of antimicrobial activity and measurements of bactericidal activity","volume":"48","author":"Sader","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.ejmech.2014.06.039","article-title":"In Vitro and In Vivo antibacterial evaluation and mechanistic study of ornithine based small cationic lipopeptides against antibiotic resistant clinical isolates","volume":"88","author":"Lohan","year":"2014","journal-title":"Eur. J. Med. Chem."},{"key":"ref_121","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_122","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/S0966-842X(00)01823-0","article-title":"The role of cationic antimicrobial peptides in innate host defences","volume":"8","author":"Hancock","year":"2000","journal-title":"Trends Microbiol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"4","DOI":"10.32614\/RJ-2015-001","article-title":"Peptides: A package for data mining of antimicrobial peptides","volume":"7","author":"Osorio","year":"2015","journal-title":"R J."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"585","DOI":"10.2174\/138920309789630589","article-title":"Anionic Antimicrobial Peptides from Eukaryotic Organisms","volume":"10","author":"Harris","year":"2009","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1002\/med.21542","article-title":"Antimicrobial peptides: Promising alternatives in the post feeding antibiotic era","volume":"39","author":"Wang","year":"2018","journal-title":"Med. Res. Rev."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1436","DOI":"10.1016\/j.bbamem.2006.03.021","article-title":"Alpha-helical antimicrobial peptides-Using a sequence template to guide structure-activity relationship studies","volume":"1758","author":"Zelezetsky","year":"2006","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"366","DOI":"10.3390\/ph8030366","article-title":"Peptides and peptidomimetics for antimicrobial drug design","volume":"8","author":"Mojsoska","year":"2015","journal-title":"Pharmaceuticals"},{"key":"ref_128","first-page":"1","article-title":"The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics","volume":"10","author":"Bonetti","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"3435","DOI":"10.3390\/ph3113435","article-title":"Spotlight on human LL-37, an immunomodulatory peptide with promising cell-penetrating properties","volume":"3","author":"Seil","year":"2010","journal-title":"Pharmaceuticals"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1007\/s10540-006-9030-z","article-title":"Melittin: A membrane-active peptide with diverse functions","volume":"27","author":"Raghuraman","year":"2007","journal-title":"Biosci. Rep."},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Ceremuga, M., Stela, M., Janik, E., Gorniak, L., Synowiec, E., Sliwinski, T., Sitarek, P., Saluk-Bijak, J., and Bijak, M. (2020). Melittin\u2014a natural peptide from bee venom which induces apoptosis in human leukaemia cells. Biomolecules, 10.","DOI":"10.3390\/biom10020247"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/S0005-2736(97)00051-5","article-title":"Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria","volume":"1327","author":"Matsuzaki","year":"1997","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1111\/j.1574-6976.2000.tb00534.x","article-title":"Class IIa bacteriocins: Biosynthesis, structure and activity","volume":"24","author":"Ennahar","year":"2000","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_134","first-page":"E7077","article-title":"Daptomycin inhibits cell envelope synthesis by interfering with fluid membrane microdomains","volume":"113","author":"Wenzel","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Zhong, G., Cheng, J., Liang, Z.C., Xu, L., Lou, W., Bao, C., Ong, Z.Y., Dong, H., Yang, Y.Y., and Fan, W. (2017). Short Synthetic \u03b2-Sheet Antimicrobial Peptides for the Treatment of Multidrug-Resistant Pseudomonas aeruginosa Burn Wound Infections. Adv. Healthc. Mater., 6.","DOI":"10.1002\/adhm.201601134"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"4957","DOI":"10.1128\/AAC.49.12.4957-4964.2005","article-title":"Antimicrobial activities and structures of two linear cationic peptide families with various amphipathic \u03b2-sheet and \u03b1-helical potentials","volume":"49","author":"Jin","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"10511","DOI":"10.1073\/pnas.0502013102","article-title":"Rational combinatorial design of pore-forming \u03b2-sheet peptides","volume":"102","author":"Rausch","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Santos-Silva, C.A., Zupin, L., Oliveira-Lima, M., Vilela, L.M., Bezerra-Neto, J.P., Ferreira-Neto, J.R., Ferreira, J.D., Oliveira-Silva, R.L., Pires, C.D., and Aburjaile, F.F. (2020). Plant Antimicrobial Peptides: State of the Art, In Silico Prediction and Perspectives in the Omics Era. Bioinform. Biol. Insights, 14.","DOI":"10.1177\/1177932220952739"},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Greco, S., Gerdol, M., Edomi, P., and Pallavicini, A. (2020). Molecular Diversity of Mytilin-Like Defense Peptides (Mollusca, Bivalvia). Antibiotics, 9.","DOI":"10.3390\/antibiotics9010037"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.peptides.2015.04.017","article-title":"Cysteine-stabilized \u03b1\u03b2 defensins: From a common fold to antibacterial activity","volume":"72","author":"Dias","year":"2015","journal-title":"Peptides"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"1","DOI":"10.5423\/PPJ.RW.08.2014.0074","article-title":"Antimicrobial cyclic peptides for plant disease control","volume":"31","author":"Lee","year":"2015","journal-title":"Plant. Pathol. J."},{"key":"ref_142","first-page":"1","article-title":"Crystal Structure of NisI in a Lipid-Free Form, the Nisin Immunity Protein, from Lactococcus lactis","volume":"62","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_143","unstructured":"Caballero, B. (2003). NISIN. Encyclopedia of Food Sciences and Nutrition, Academic Press. [2nd ed.]."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"10372","DOI":"10.1021\/bi034490u","article-title":"Structure and dynamics of the lantibiotic mutacin 1140","volume":"42","author":"Smith","year":"2003","journal-title":"Biochemistry"},{"key":"ref_145","first-page":"1","article-title":"Bactofencin A, a new type of cationic bacteriocin with Unusual Immunity","volume":"4","author":"Cotter","year":"2013","journal-title":"MBio"},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"Rubinchik, E., and Dugourd, D. (2011). Omiganan Pentahydrochloride: A Novel, Broad-Spectrum Antimicrobial Peptide for Topical Use, Wiley-VCH Verlag GmbH & Co, Boschstr.","DOI":"10.1002\/9783527636730.ch7"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"4918","DOI":"10.1128\/AAC.00202-11","article-title":"Easy strategy to increase salt resistance of antimicrobial peptides","volume":"55","author":"Yu","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_148","unstructured":"National Center for Biotechnology Information (2021, June 03). PubChem Compound Summary for CID 16131446, Omiganan Pentahydrochloride, Available online: https:\/\/pubchem.ncbi.nlm.nih.gov\/compound\/Omiganan-pentahydrochloride."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1007\/s10989-020-10110-x","article-title":"Antimicrobial Peptides as Potential Therapeutic Agents: A Review","volume":"27","author":"Datta","year":"2021","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.2174\/138945012802002410","article-title":"Bacterial Cell Wall Compounds as Promising Targets of Antimicrobial Agents I. Antimicrobial Peptides and Lipopolyamines","volume":"13","author":"Kowalski","year":"2012","journal-title":"Curr. Drug Targets"},{"key":"ref_151","doi-asserted-by":"crossref","unstructured":"Malanovic, N., and Lohner, K. (2016). Antimicrobial Peptides Targeting Gram-Positive Bacteria. Pharmaceuticals, 9.","DOI":"10.3390\/ph9030059"},{"key":"ref_152","first-page":"139","article-title":"Amino Acid Composition Determines Peptide Activity Spectrum and Hot-Spot-Based Design of Merecidin","volume":"176","author":"Ren","year":"2019","journal-title":"Physiol. Behav."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"7738","DOI":"10.1074\/jbc.M111.303602","article-title":"Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions","volume":"287","author":"Yin","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1093\/femsre\/fuv008","article-title":"Bacterial membrane lipids: Diversity in structures and pathways","volume":"40","author":"Sohlenkamp","year":"2015","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"33854","DOI":"10.1074\/jbc.M805171200","article-title":"On the mechanism of pore formation by melittin","volume":"283","author":"Mika","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"11856","DOI":"10.1021\/bi980539y","article-title":"Relationship of Membrane Curvature to the Formation of Pores by Magainin 2","volume":"37","author":"Matsuzaki","year":"1998","journal-title":"Biochemistry"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1111\/j.1574-6968.1998.tb12896.x","article-title":"Mechanism of antimicrobial action of indolicidin","volume":"160","author":"Subbalakshmi","year":"1998","journal-title":"FEMS Microbiol. Lett."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/15\/7927\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:34:40Z","timestamp":1760164480000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/15\/7927"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,7,25]]},"references-count":157,"journal-issue":{"issue":"15","published-online":{"date-parts":[[2021,8]]}},"alternative-id":["ijms22157927"],"URL":"https:\/\/doi.org\/10.3390\/ijms22157927","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,7,25]]}}}