{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T14:15:49Z","timestamp":1772115349484,"version":"3.50.1"},"reference-count":68,"publisher":"Oxford University Press (OUP)","issue":"5","license":[{"start":{"date-parts":[[2021,1,27]],"date-time":"2021-01-27T00:00:00Z","timestamp":1611705600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia\u2014Minist\u00e9rio da Ci\u00eancia, Tecnologia e Ensino Superior"},{"name":"Marie Sk\u0142odowska-Curie, Research and Innovation Staff Exchange","award":["H2020-MSCA-RISE-2014"],"award-info":[{"award-number":["H2020-MSCA-RISE-2014"]}]},{"name":"Marie Sk\u0142odowska-Curie, Research and Innovation Staff Exchange","award":["644167"],"award-info":[{"award-number":["644167"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,4,13]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Objectives<\/jats:title>\n                  <jats:p>The number of bacterial pathogens resistant to the currently available antibiotics has dramatically increased, with antimicrobial peptides (AMPs) being among the most promising potential new drugs. In this study, the applicability and mechanisms of action of Pa-MAP 2 and Pa-MAP 1.9, two AMPs synthetically designed based on a natural AMP template, were evaluated.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Methods<\/jats:title>\n                  <jats:p>Pa-MAP 2 and Pa-MAP 1.9 were tested against a clinically isolated multidrug-resistant (MDR) Escherichia coli strain. Biophysical approaches were used to evaluate the preference of both peptides for specific lipid membranes, and bacterial surface changes imaged by atomic force microscopy (AFM). The efficacy of both peptides was assessed both in vitro and in vivo.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Results<\/jats:title>\n                  <jats:p>Experimental results showed that both peptides have antimicrobial activity against the E. coli MDR strain. Zeta potential and surface plasmon resonance assays showed that they interact extensively with negatively charged membranes, changing from a random coil structure, when free in solution, to an \u03b1-helical structure after membrane interaction. The antibacterial efficacy was evaluated in vitro, by several techniques, and in vivo, using a wound infection model, showing a concentration-dependent antibacterial effect. Different membrane properties were evaluated to understand the mechanism underlying peptide action, showing that both promote destabilization of the bacterial surface, as imaged by AFM, and change properties such as membrane surface and dipole potential.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Conclusions<\/jats:title>\n                  <jats:p>Despite their similarity, data indicate that the mechanisms of action of the peptides are different, with Pa-MAP 1.9 being more effective than Pa-MAP 2. These results highlight their potential use as antimicrobial agents against MDR bacteria.<\/jats:p>\n               <\/jats:sec>","DOI":"10.1093\/jac\/dkaa560","type":"journal-article","created":{"date-parts":[[2020,12,23]],"date-time":"2020-12-23T20:19:25Z","timestamp":1608754765000},"page":"1174-1186","source":"Crossref","is-referenced-by-count":9,"title":["Polyalanine peptide variations may have different mechanisms of action against multidrug-resistant bacterial pathogens"],"prefix":"10.1093","volume":"76","author":[{"given":"M\u00e1rio R","family":"Fel\u00edcio","sequence":"first","affiliation":[{"name":"Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Avenida Professor Egas Moniz, 1649-028 Lisboa, Portugal"}]},{"given":"Gislaine G O S","family":"Silveira","sequence":"additional","affiliation":[{"name":"S-Inova Biotech, P\u00f3s-gradua\u00e7\u00e3o em Biotecnologia, Universidade Cat\u00f3lica Dom Bosco, Campo Grande, MS, Brazil"}]},{"given":"Karen G N","family":"Oshiro","sequence":"additional","affiliation":[{"name":"S-Inova Biotech, P\u00f3s-gradua\u00e7\u00e3o em Biotecnologia, Universidade Cat\u00f3lica Dom Bosco, Campo Grande, MS, Brazil"},{"name":"Programa de P\u00f3s-Gradua\u00e7\u00e3o em Patologia Molecular, Universidade de Bras\u00edlia, Bras\u00edlia, DF, Brazil"}]},{"given":"Beatriz T","family":"Meneguetti","sequence":"additional","affiliation":[{"name":"S-Inova Biotech, P\u00f3s-gradua\u00e7\u00e3o em Biotecnologia, Universidade Cat\u00f3lica Dom Bosco, Campo Grande, MS, Brazil"}]},{"given":"Oct\u00e1vio L","family":"Franco","sequence":"additional","affiliation":[{"name":"S-Inova Biotech, P\u00f3s-gradua\u00e7\u00e3o em Biotecnologia, Universidade Cat\u00f3lica Dom Bosco, Campo Grande, MS, Brazil"},{"name":"Programa de P\u00f3s-Gradua\u00e7\u00e3o em Patologia Molecular, Universidade de Bras\u00edlia, Bras\u00edlia, DF, Brazil"},{"name":"Centro de An\u00e1lises Prote\u00f4micas e Bioqu\u00edmicas, P\u00f3s-gradua\u00e7\u00e3o em Ci\u00eancias Gen\u00f4micas e Biotecnologia, Universidade Cat\u00f3lica de Bras\u00edlia, Bras\u00edlia, DF, Brazil"}]},{"given":"Nuno C","family":"Santos","sequence":"additional","affiliation":[{"name":"Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Avenida Professor Egas Moniz, 1649-028 Lisboa, Portugal"}]},{"given":"S\u00f3nia","family":"Gon\u00e7alves","sequence":"additional","affiliation":[{"name":"Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Avenida Professor Egas Moniz, 1649-028 Lisboa, Portugal"}]}],"member":"286","published-online":{"date-parts":[[2021,1,27]]},"reference":[{"key":"2021041608543548200_dkaa560-B1","doi-asserted-by":"crossref","first-page":"2419","DOI":"10.1016\/j.bbamem.2013.06.009","article-title":"rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures","volume":"1828","author":"Domingues","year":"2013","journal-title":"Biochim Biophys Acta"},{"key":"2021041608543548200_dkaa560-B2","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1038\/499394a","article-title":"Antibiotic resistance: the last resort","volume":"499","author":"McKenna","year":"2013","journal-title":"Nature"},{"key":"2021041608543548200_dkaa560-B3","doi-asserted-by":"crossref","first-page":"e01541-16","DOI":"10.1128\/mBio.01541-16","article-title":"Antibiotic resistance and regulation of the Gram-negative bacterial outer membrane barrier by host innate immune molecules","volume":"7","author":"Miller","year":"2016","journal-title":"mBio"},{"key":"2021041608543548200_dkaa560-B4","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1016\/j.mib.2013.06.013","article-title":"Bacterial biofilm development as a multicellular adaptation: antibiotic resistance and new therapeutic strategies","volume":"16","author":"de la Fuente-N\u00fa\u00f1ez","year":"2013","journal-title":"Curr Opin Microbiol"},{"key":"2021041608543548200_dkaa560-B5","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1016\/j.bbamem.2012.02.012","article-title":"Evaluation of the membrane lipid selectivity of the pea defensin Psd1","volume":"1818","author":"Gon\u00e7alves","year":"2012","journal-title":"Biochim Biophys Acta"},{"key":"2021041608543548200_dkaa560-B6","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s12275-017-6452-1","article-title":"The therapeutic applications of antimicrobial peptides (AMPs): a patent review","volume":"55","author":"Kang","year":"2017","journal-title":"J Microbiol"},{"key":"2021041608543548200_dkaa560-B7","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1021\/acsinfecdis.6b00045","article-title":"Contribution of amphipathicity and hydrophobicity to the antimicrobial activity and cytotoxicity of \u03b2-hairpin peptides","volume":"2","author":"Edwards","year":"2016","journal-title":"ACS Infect Dis"},{"key":"2021041608543548200_dkaa560-B8","doi-asserted-by":"crossref","first-page":"249","DOI":"10.3389\/fcimb.2017.00249","article-title":"Psd1 effects on Candida albicans planktonic cells and biofilms","volume":"7","author":"Gon\u00e7alves","year":"2017","journal-title":"Front Cell Infect Microbiol"},{"key":"2021041608543548200_dkaa560-B9","doi-asserted-by":"crossref","first-page":"3078","DOI":"10.1016\/j.bbamem.2015.02.017","article-title":"Understanding bacterial resistance to antimicrobial peptides: from the surface to deep inside","volume":"1848","author":"Maria-Neto","year":"2015","journal-title":"Biochim Biophys Acta"},{"key":"2021041608543548200_dkaa560-B10","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1128\/CMR.00056-05","article-title":"Peptide antimicrobial agents","volume":"19","author":"Jenssen","year":"2006","journal-title":"Clin Microbiol Rev"},{"key":"2021041608543548200_dkaa560-B11","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.chembiol.2016.12.009","article-title":"Glycan alteration imparts cellular resistance to a membrane-lytic anticancer peptide","volume":"24","author":"Ishikawa","year":"2017","journal-title":"Cell Chem Biol"},{"key":"2021041608543548200_dkaa560-B12","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1038\/nrmicro2095","article-title":"Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations","volume":"7","author":"Melo","year":"2009","journal-title":"Nat Rev Microbiol"},{"key":"2021041608543548200_dkaa560-B13","doi-asserted-by":"crossref","first-page":"2500","DOI":"10.1016\/j.bbamem.2007.05.023","article-title":"Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (ceragenins)","volume":"1768","author":"Epand","year":"2007","journal-title":"Biochim Biophys Acta"},{"key":"2021041608543548200_dkaa560-B14","doi-asserted-by":"crossref","first-page":"1957","DOI":"10.1016\/j.bbamem.2011.03.016","article-title":"Choosing membrane mimetics for NMR structural studies of transmembrane proteins","volume":"1808","author":"Warschawski","year":"2011","journal-title":"Biochim Biophys Acta"},{"key":"2021041608543548200_dkaa560-B15","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1586\/14787210.5.6.951","article-title":"Alternative mechanisms of action of cationic antimicrobial peptides on bacteria","volume":"5","author":"Hale","year":"2007","journal-title":"Expert Rev Anti Infect Ther"},{"key":"2021041608543548200_dkaa560-B16","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.pharmthera.2017.04.002","article-title":"Antimicrobial peptides: role in human disease and potential as immunotherapies","volume":"178","author":"de la Fuente-N\u00fa\u00f1ez","year":"2017","journal-title":"Pharmacol Ther"},{"key":"2021041608543548200_dkaa560-B17","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.cis.2013.06.009","article-title":"Effect of hydrophobic modifications in antimicrobial peptides","volume":"205","author":"Schmidtchen","year":"2014","journal-title":"Adv Colloid Interface Sci"},{"key":"2021041608543548200_dkaa560-B18","doi-asserted-by":"crossref","first-page":"24015","DOI":"10.1074\/jbc.M009691200","article-title":"Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria","volume":"276","author":"Friedrich","year":"2001","journal-title":"J Biol Chem"},{"key":"2021041608543548200_dkaa560-B19","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":"2021041608543548200_dkaa560-B20","doi-asserted-by":"crossref","first-page":"e28549","DOI":"10.1371\/journal.pone.0028549","article-title":"Prediction of antibacterial activity from physicochemical properties of antimicrobial peptides","volume":"6","author":"Melo","year":"2011","journal-title":"PLoS One"},{"key":"2021041608543548200_dkaa560-B21","doi-asserted-by":"crossref","first-page":"e47047","DOI":"10.1371\/journal.pone.0047047","article-title":"Structural and functional characterization of a multifunctional alanine-rich peptide analogue from Pleuronectes americanus","volume":"7","author":"Migliolo","year":"2012","journal-title":"PLoS One"},{"key":"2021041608543548200_dkaa560-B22","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.peptides.2013.02.001","article-title":"In vivo antimicrobial evaluation of an alanine-rich peptide derived from Pleuronectes americanus","volume":"42","author":"Teixeira","year":"2013","journal-title":"Peptides"},{"key":"2021041608543548200_dkaa560-B23","doi-asserted-by":"crossref","first-page":"21385","DOI":"10.1038\/srep21385","article-title":"A polyalanine peptide derived from polar fish with anti-infectious activities","volume":"6","author":"Cardoso","year":"2016","journal-title":"Sci Rep"},{"key":"2021041608543548200_dkaa560-B24","doi-asserted-by":"crossref","first-page":"1488","DOI":"10.1016\/j.bbamem.2016.04.003","article-title":"Structural and functional evaluation of the palindromic alanine-rich antimicrobial peptide Pa-MAP2","volume":"1858","author":"Migliolo","year":"2016","journal-title":"Biochim Biophys Acta"},{"key":"2021041608543548200_dkaa560-B25","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1016\/j.bbamem.2019.03.016","article-title":"Selective antibacterial activity of the cationic peptide PaDBS1R6 against Gram-negative bacteria","volume":"1861","author":"Fensterseifer","year":"2019","journal-title":"Biochim Biophys Acta Biomembr"},{"key":"2021041608543548200_dkaa560-B26","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.bbamem.2018.08.001","article-title":"Fast and potent bactericidal membrane lytic activity of PaDBS1R1, a novel cationic antimicrobial peptide","volume":"1861","author":"Irazazabal","year":"2019","journal-title":"Biochim Biophys Acta"},{"key":"2021041608543548200_dkaa560-B27","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.bbamem.2018.12.020","article-title":"Psd2 pea defensin shows a preference for mimetic membrane rafts enriched with glucosylceramide and ergosterol","volume":"1861","author":"Amaral","year":"2019","journal-title":"Biochim Biophys Acta"},{"key":"2021041608543548200_dkaa560-B28","doi-asserted-by":"crossref","first-page":"27536","DOI":"10.1074\/jbc.M110.130955","article-title":"Escherichia coli cell surface perturbation and disruption induced by antimicrobial peptides BP100 and pepR","volume":"285","author":"Alves","year":"2010","journal-title":"J Biol Chem"},{"key":"2021041608543548200_dkaa560-B29","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1021\/cb500640t","article-title":"Understanding dengue virus capsid protein disordered N-terminus and pep14-23-based inhibition","volume":"10","author":"Faustino","year":"2015","journal-title":"ACS Chem Biol"},{"key":"2021041608543548200_dkaa560-B30","doi-asserted-by":"crossref","first-page":"2733","DOI":"10.1038\/nprot.2006.229","article-title":"Determination of the folding of proteins as a function of denaturants, osmolytes or ligands using circular dichroism","volume":"1","author":"Greenfield","year":"2006","journal-title":"Nat Protoc"},{"key":"2021041608543548200_dkaa560-B31","doi-asserted-by":"crossref","first-page":"2876","DOI":"10.1038\/nprot.2006.202","article-title":"Using circular dichroism spectra to estimate protein secondary structure","volume":"1","author":"Greenfield","year":"2006","journal-title":"Nat Protoc"},{"key":"2021041608543548200_dkaa560-B32","doi-asserted-by":"crossref","first-page":"e8385","DOI":"10.1371\/journal.pone.0008385","article-title":"rBPI(21) promotes lipopolysaccharide aggregation and exerts its antimicrobial effects by (hemi)fusion of PG-containing membranes","volume":"4","author":"Domingues","year":"2009","journal-title":"PLoS One"},{"key":"2021041608543548200_dkaa560-B33","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1007\/s00249-010-0661-4","article-title":"Using zeta-potential measurements to quantify peptide partition to lipid membranes","volume":"40","author":"Freire","year":"2011","journal-title":"Eur Biophys J"},{"key":"2021041608543548200_dkaa560-B34","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/j.actbio.2013.08.043","article-title":"Design of imperfectly amphipathic \u03b1-helical antimicrobial peptides with enhanced cell selectivity","volume":"10","author":"Zhu","year":"2014","journal-title":"Acta Biomater"},{"key":"2021041608543548200_dkaa560-B35","doi-asserted-by":"crossref","first-page":"2434","DOI":"10.1016\/S0006-3495(98)77951-2","article-title":"Intramembrane molecular dipoles affect the membrane insertion and folding of a model amphiphilic peptide","volume":"74","author":"Cladera","year":"1998","journal-title":"Biophys J"},{"key":"2021041608543548200_dkaa560-B36","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1002\/bip.22088","article-title":"Lipid composition is a determinant for human defensin HNP1 selectivity","volume":"98","author":"Gon\u00e7alves","year":"2012","journal-title":"Biopolymers"},{"key":"2021041608543548200_dkaa560-B37","doi-asserted-by":"crossref","first-page":"3708","DOI":"10.1128\/AAC.00380-10","article-title":"Depolarization, bacterial membrane composition, and the antimicrobial action of ceragenins","volume":"54","author":"Epand","year":"2010","journal-title":"Antimicrob Agents Chemother"},{"key":"2021041608543548200_dkaa560-B38","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.peptides.2014.10.019","article-title":"Effects of cyclotides against cutaneous infections caused by Staphylococcus aureus","volume":"63","author":"Fensterseifer","year":"2015","journal-title":"Peptides"},{"key":"2021041608543548200_dkaa560-B39","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1016\/j.bbamem.2014.11.001","article-title":"Monitoring antibacterial permeabilization in real time using time-resolved flow cytometry","volume":"1848","author":"Freire","year":"2015","journal-title":"Biochim Biophys Acta"},{"key":"2021041608543548200_dkaa560-B40","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1002\/cyto.a.20069","article-title":"Mechanism and use of the commercially available viability stain, BacLight","volume":"61A","author":"Stocks","year":"2004","journal-title":"Cytometry"},{"key":"2021041608543548200_dkaa560-B41","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1016\/j.nano.2013.11.002","article-title":"Antimicrobial protein rBPI21-induced surface changes on Gram-negative and Gram-positive bacteria","volume":"10","author":"Domingues","year":"2014","journal-title":"Nanomedicine"},{"key":"2021041608543548200_dkaa560-B42","doi-asserted-by":"crossref","first-page":"2013","DOI":"10.1002\/cbic.201300274","article-title":"The antimicrobial activity of Sub3 is dependent on membrane binding and cell-penetrating ability","volume":"14","author":"Torcato","year":"2013","journal-title":"ChemBioChem"},{"key":"2021041608543548200_dkaa560-B43","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":"2021041608543548200_dkaa560-B44","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1021\/bi0620297","article-title":"Structure and mechanism of action of the antimicrobial peptide piscidin","volume":"46","author":"Campagna","year":"2007","journal-title":"Biochemistry"},{"key":"2021041608543548200_dkaa560-B45","doi-asserted-by":"crossref","first-page":"1984","DOI":"10.1128\/AAC.02146-15","article-title":"Destabilization of \u03b1-helical structure in solution improves bactericidal activity of antimicrobial peptides: opposite effects on bacterial and viral targets","volume":"60","author":"Ulaeto","year":"2016","journal-title":"Antimicrob Agents Chemother"},{"key":"2021041608543548200_dkaa560-B46","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.actbio.2016.01.019","article-title":"The effects of LPS on the activity of Trp-containing antimicrobial peptides against Gram-negative bacteria and endotoxin neutralization","volume":"33","author":"Shang","year":"2016","journal-title":"Acta Biomater"},{"key":"2021041608543548200_dkaa560-B47","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.colsurfb.2017.02.003","article-title":"Lipid selectivity in novel antimicrobial peptides: implication on antimicrobial and hemolytic activity","volume":"153","author":"Maturana","year":"2017","journal-title":"Colloids Surfaces B Biointerfaces"},{"key":"2021041608543548200_dkaa560-B48","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.molstruc.2017.06.018","article-title":"Antimicrobial peptides interact with peptidoglycan","volume":"1146","author":"Neelay","year":"2017","journal-title":"J Mol Struct"},{"key":"2021041608543548200_dkaa560-B49","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/S1473-3099(01)00092-5","article-title":"Cationic peptides: effectors in innate immunity and novel antimicrobials","volume":"1","author":"Hancock","year":"2001","journal-title":"Lancet Infect Dis"},{"key":"2021041608543548200_dkaa560-B50","doi-asserted-by":"crossref","first-page":"eaan4044","DOI":"10.1126\/scitranslmed.aan4044","article-title":"The antimicrobial peptide SAAP-148 combats drug-resistant bacteria and biofilms","volume":"10","author":"de Breij","year":"2018","journal-title":"Sci Transl Med"},{"key":"2021041608543548200_dkaa560-B51","doi-asserted-by":"crossref","first-page":"5156","DOI":"10.1073\/pnas.93.10.5156","article-title":"Inducible expression of an antibiotic peptide gene in lipopolysaccharide-challenged tracheal epithelial cells","volume":"93","author":"Diamond","year":"1996","journal-title":"Proc Natl Acad Sci USA"},{"key":"2021041608543548200_dkaa560-B52","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":"2021041608543548200_dkaa560-B53","doi-asserted-by":"crossref","first-page":"8028","DOI":"10.1016\/j.biomaterials.2014.06.005","article-title":"Antimicrobial potency and selectivity of simplified symmetric-end peptides","volume":"35","author":"Dong","year":"2014","journal-title":"Biomaterials"},{"key":"2021041608543548200_dkaa560-B54","doi-asserted-by":"crossref","first-page":"1944","DOI":"10.1016\/j.bbamem.2015.02.019","article-title":"AMPs and OMPs: is the folding and bilayer insertion of \u03b2-stranded outer membrane proteins governed by the same biophysical principles as for \u03b1-helical antimicrobial peptides?","volume":"1848","author":"Strandberg","year":"2015","journal-title":"Biochim Biophys Acta"},{"key":"2021041608543548200_dkaa560-B55","doi-asserted-by":"crossref","first-page":"3317","DOI":"10.1128\/AAC.44.12.3317-3321.2000","article-title":"Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa","volume":"44","author":"Zhang","year":"2000","journal-title":"Antimicrob Agents Chemother"},{"key":"2021041608543548200_dkaa560-B56","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.bbrc.2018.02.176","article-title":"Interaction of MreB-derived antimicrobial peptides with membranes","volume":"498","author":"Saikia","year":"2018","journal-title":"Biochem Biophys Res Commun"},{"key":"2021041608543548200_dkaa560-B57","doi-asserted-by":"crossref","first-page":"e98935","DOI":"10.1371\/journal.pone.0098935","article-title":"Design of embedded-hybrid antimicrobial peptides with enhanced cell selectivity and anti-biofilm activity","volume":"9","author":"Xu","year":"2014","journal-title":"PLoS One"},{"key":"2021041608543548200_dkaa560-B58","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":"2021041608543548200_dkaa560-B59","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1128\/MMBR.67.4.593-656.2003","article-title":"Molecular basis of bacterial outer membrane permeability revisited","volume":"67","author":"Nikaido","year":"2003","journal-title":"Microbiol Mol Biol Rev"},{"key":"2021041608543548200_dkaa560-B60","doi-asserted-by":"crossref","first-page":"1536","DOI":"10.1074\/jbc.RA117.000125","article-title":"Mechanisms of bacterial membrane permeabilization by crotalicidin (Ctn) and its fragment Ctn(15-34), antimicrobial peptides from rattlesnake venom","volume":"293","author":"P\u00e9rez-Peinado","year":"2018","journal-title":"J Biol Chem"},{"key":"2021041608543548200_dkaa560-B61","doi-asserted-by":"crossref","first-page":"e0151694","DOI":"10.1371\/journal.pone.0151694","article-title":"A rapid and quantitative flow cytometry method for the analysis of membrane disruptive antimicrobial activity","volume":"11","author":"O\u2019Brien-Simpson","year":"2016","journal-title":"PLoS One"},{"key":"2021041608543548200_dkaa560-B62","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1007\/978-1-4939-8894-5_13","volume-title":"Atomic Force Microscopy. Methods in Molecular Biology","author":"Domingues","year":"2019"},{"key":"2021041608543548200_dkaa560-B63","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1002\/psc.2708","article-title":"Peptide IDR-1018: modulating the immune system and targeting bacterial biofilms to treat antibiotic-resistant bacterial infections","volume":"21","author":"Mansour","year":"2015","journal-title":"J Pept Sci"},{"key":"2021041608543548200_dkaa560-B64","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1038\/s42003-018-0224-2","article-title":"Structure-function-guided exploration of the antimicrobial peptide polybia-CP identifies activity determinants and generates synthetic therapeutic candidates","volume":"1","author":"Torres","year":"2018","journal-title":"Commun Biol"},{"key":"2021041608543548200_dkaa560-B65","doi-asserted-by":"crossref","first-page":"43610","DOI":"10.1038\/srep43610","article-title":"Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides","volume":"7","author":"Mathieu","year":"2017","journal-title":"Sci Rep"},{"key":"2021041608543548200_dkaa560-B66","doi-asserted-by":"crossref","first-page":"1409","DOI":"10.1111\/jam.12796","article-title":"Study of surface damage on cell envelope assessed by AFM and flow cytometry of Lactobacillus plantarum exposed to ethanol and dehydration","volume":"118","author":"Bravo-Ferrada","year":"2015","journal-title":"J Appl Microbiol"},{"key":"2021041608543548200_dkaa560-B67","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1016\/j.bbagen.2013.11.019","article-title":"Atomic Force Microscopy and pharmacology: from microbiology to cancerology","volume":"1840","author":"Pillet","year":"2014","journal-title":"Biochim Biophys Acta"},{"key":"2021041608543548200_dkaa560-B68","doi-asserted-by":"crossref","first-page":"775","DOI":"10.3389\/fmicb.2017.00775","article-title":"New potent membrane-targeting antibacterial peptides from viral capsid proteins","volume":"8","author":"Dias","year":"2017","journal-title":"Front Microbiol"}],"container-title":["Journal of Antimicrobial Chemotherapy"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/jac\/article-pdf\/76\/5\/1174\/37042067\/dkaa560.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/academic.oup.com\/jac\/article-pdf\/76\/5\/1174\/37042067\/dkaa560.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,4,17]],"date-time":"2021-04-17T07:37:34Z","timestamp":1618645054000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jac\/article\/76\/5\/1174\/6121183"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,1,27]]},"references-count":68,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2021,1,27]]},"published-print":{"date-parts":[[2021,4,13]]}},"URL":"https:\/\/doi.org\/10.1093\/jac\/dkaa560","relation":{},"ISSN":["0305-7453","1460-2091"],"issn-type":[{"value":"0305-7453","type":"print"},{"value":"1460-2091","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2021,5,1]]},"published":{"date-parts":[[2021,1,27]]}}}