{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,18]],"date-time":"2026-10-18T05:34:04Z","timestamp":1792301644906,"version":"4.4.0"},"reference-count":55,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2017,10,1]],"date-time":"2017-10-01T00:00:00Z","timestamp":1506816000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2017,6,5]],"date-time":"2017-06-05T00:00:00Z","timestamp":1496620800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"published-print":{"date-parts":[[2017,10]]},"DOI":"10.1016\/j.bbamem.2017.06.001","type":"journal-article","created":{"date-parts":[[2017,6,3]],"date-time":"2017-06-03T18:18:21Z","timestamp":1496513901000},"page":"1796-1804","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":36,"title":["Investigations into the killing activity of an antimicrobial peptide active against extensively antibiotic-resistant K. pneumon iae and P. aeruginosa"],"prefix":"10.1016","volume":"1859","author":[{"given":"Hessel","family":"van der Weide","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8144-7186","authenticated-orcid":false,"given":"Jlenia","family":"Brunetti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alessandro","family":"Pini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luisa","family":"Bracci","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chiara","family":"Ambrosini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pietro","family":"Lupetti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eugenio","family":"Paccagnini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mariangela","family":"Gentile","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Bernini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neri","family":"Niccolai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Denise Vermeulen-de","family":"Jongh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irma A.J.M.","family":"Bakker-Woudenberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wil H.F.","family":"Goessens","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John P.","family":"Hays","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chiara","family":"Falciani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamem.2017.06.001_bb0005","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1093\/jac\/dkg028","article-title":"An international survey of the antimicrobial susceptibility of pathogens from uncomplicated urinary tract infections: the ECO\u00b7SENS Project","volume":"51","author":"Kahlmeter","year":"2003","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0010","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1093\/cid\/cit734","article-title":"Healthcare-associated pneumonia does not accurately identify potentially resistant pathogens: a systematic review and meta-analysis","volume":"58","author":"Chalmers","year":"2014","journal-title":"Clin. Infect. Dis."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0015","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.1517\/14656566.2014.914172","article-title":"Multidrug-resistant and extensively drug-resistant Gram-negative pathogens: current and emerging therapeutic approaches","volume":"15","author":"Karaiskos","year":"2014","journal-title":"Expert. Opin. Pharmacother."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0020","first-page":"25","article-title":"Antibiotics and bacterial resistance in the 21st century","volume":"6","author":"Fair","year":"2014","journal-title":"Perspect. Med. Chem."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0025","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1586\/14787210.6.5.751","article-title":"Clinical and economic burden of antimicrobial resistance","volume":"6","author":"Maragakis","year":"2008","journal-title":"Expert Rev. Anti-Infect. Ther."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0030","series-title":"Antimicrobial Resistance: Global Report on Surveillance","author":"World Health Organization","year":"2014"},{"key":"10.1016\/j.bbamem.2017.06.001_bb0035","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.1038\/nbt1267","article-title":"Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies","volume":"24","author":"Hancock","year":"2006","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0040","doi-asserted-by":"crossref","DOI":"10.1016\/j.pharmthera.2017.04.002","article-title":"Antimicrobial peptides: Role in human disease and potential as immunotherapies","author":"de la Fuente-N\u00fa\u00f1ez","year":"2017","journal-title":"Pharmacol Ther."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0045","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":"10.1016\/j.bbamem.2017.06.001_bb0050","doi-asserted-by":"crossref","first-page":"R14","DOI":"10.1016\/j.cub.2015.11.017","article-title":"Antimicrobial peptides","volume":"26","author":"Zhang","year":"2016","journal-title":"Curr. Biol."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0055","doi-asserted-by":"crossref","first-page":"641","DOI":"10.2174\/138920371408131227155308","article-title":"The development of antimicrobial peptides as new antibacterial drugs","volume":"14","author":"Roscia","year":"2013","journal-title":"Curr. Protein Pept. Sci."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0060","doi-asserted-by":"crossref","first-page":"613","DOI":"10.2174\/1568026616666160713143017","article-title":"Models of in-vivo bacterial infections for the development of antimicrobial peptide-based drugs","volume":"17","author":"Brunetti","year":"2017","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0065","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/S0005-2736(99)00198-4","article-title":"Diversity of antimicrobial peptides and their mechanisms of action","volume":"1462","author":"Epand","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2017.06.001_bb0070","doi-asserted-by":"crossref","first-page":"1529","DOI":"10.1016\/j.bbamem.2006.07.001","article-title":"Detergent-like actions of linear amphipathic cationic antimicrobial peptides","volume":"1758","author":"Bechinger","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2017.06.001_bb0075","doi-asserted-by":"crossref","first-page":"4471","DOI":"10.1007\/s00018-016-2302-2","article-title":"Morphological and ultrastructural changes in bacterial cells as an indicator of antibacterial mechanism of action","volume":"73","author":"Cushnie","year":"2016","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0080","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":"10.1016\/j.bbamem.2017.06.001_bb0085","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1039\/c1np00022e","article-title":"Antibiotic activities of host defense peptides: more to it than lipid bilayer perturbation","volume":"28","author":"Wilmes","year":"2011","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0090","doi-asserted-by":"crossref","first-page":"2","DOI":"10.2174\/138920109787048616","article-title":"Antibiotics: mode of action, biosynthesis and bioengineering","volume":"10","author":"Bierbaum","year":"2009","journal-title":"Curr. Pharm. Biotechnol."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0095","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1002\/psc.1319","article-title":"Bacterial membrane lipids in the action of antimicrobial agents","volume":"17","author":"Epand","year":"2011","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0100","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1039\/b900278m","article-title":"Domains in bacterial membranes and the action of antimicrobial agents","volume":"5","author":"Epand","year":"2009","journal-title":"Mol. BioSyst."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0105","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1002\/psc.2978","article-title":"Synergistic activity profile of an antimicrobial peptide against multidrug-resistant and extensively drug-resistant strains of Gram-negative bacterial pathogens","volume":"23","author":"Pollini","year":"2017","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0110","doi-asserted-by":"crossref","first-page":"26077","DOI":"10.1038\/srep26077","article-title":"In vitro and in vivo efficacy, toxicity, bio-distribution and resistance selection of a novel antibacterial drug candidate","volume":"6","author":"Brunetti","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0115","doi-asserted-by":"crossref","first-page":"25742","DOI":"10.1074\/jbc.M116.750257","article-title":"Immunomodulatory and anti-inflammatory activity in vitro and in vivo of a novel antimicrobial candidate","volume":"291","author":"Brunetti","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0120","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1007\/s00726-011-1103-z","article-title":"Efficacy and toxicity of the antimicrobial peptide M33 produced with different counter-ions","volume":"43","author":"Pini","year":"2012","journal-title":"Amino Acids"},{"key":"10.1016\/j.bbamem.2017.06.001_bb0125","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1096\/fj.09-145474","article-title":"A novel tetrabranched antimicrobial peptide that neutralizes bacterial lipopolysaccharide and prevents septic shock in vivo","volume":"24","author":"Pini","year":"2010","journal-title":"FASEB J."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0130","doi-asserted-by":"crossref","first-page":"46590","DOI":"10.1074\/jbc.M308615200","article-title":"Synthetic peptides in the form of dendrimers become resistant to protease activity","volume":"278","author":"Bracci","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0135","doi-asserted-by":"crossref","first-page":"2981","DOI":"10.1093\/jac\/dkv244","article-title":"Loss of LPS is involved in the virulence and resistance to colistin of colistin-resistant Acinetobacter nosocomialis mutants selected in vitro","volume":"70","author":"Vila-Farr\u00e9s","year":"2015","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0140","article-title":"Breakpoint tables for interpretation of MICs and zone diameters","author":"The European Committee on Antimicrobial Susceptibility Testing","year":"2017","journal-title":"Version 7.1"},{"key":"10.1016\/j.bbamem.2017.06.001_bb0145","doi-asserted-by":"crossref","first-page":"2582","DOI":"10.1093\/jac\/dkq374","article-title":"Time-kill kinetics of anti-tuberculosis drugs, and emergence of resistance, in relation to metabolic activity of Mycobacterium tuberculosis","volume":"65","author":"de Steenwinkel","year":"2010","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0150","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1006\/jmbi.1997.1284","article-title":"Torsion angle dynamics for NMR structure calculation with the new program DYANA","volume":"273","author":"G\u00fcntert","year":"1997","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0155","series-title":"Basic and Clinical Pharmacology","article-title":"Clinical use of antimicrobial agents (chapter 51)","author":"Lampiris","year":"2012"},{"key":"10.1016\/j.bbamem.2017.06.001_bb0160","doi-asserted-by":"crossref","first-page":"7107","DOI":"10.1128\/IAI.72.12.7107-7114.2004","article-title":"Capsule polysaccharide mediates bacterial resistance to antimicrobial peptides","volume":"72","author":"Campos","year":"2004","journal-title":"Infect. Immun."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0165","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1016\/S1473-3099(06)70580-1","article-title":"Colistin: the re-emerging antibiotic for multidrug-resistant Gram-negative bacterial infections","volume":"6","author":"Li","year":"2006","journal-title":"Lancet Infect. Dis."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0170","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1128\/AAC.00871-13","article-title":"Clinical experience of colistin-glycopeptide combination in critically ill patients infected with Gram-negative bacteria","volume":"58","author":"Petrosillo","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0175","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.ijantimicag.2014.02.016","article-title":"Colistin resistance in Klebsiella pneumoniae","volume":"44","author":"Ah","year":"2014","journal-title":"Int. J. Antimicrob. Agents"},{"key":"10.1016\/j.bbamem.2017.06.001_bb0180","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1016\/j.cmi.2015.05.022","article-title":"Contemporary resistance trends and mechanisms for the old antibiotics colistin, temocillin, fosfomycin, mecillinam and nitrofurantoin","volume":"21","author":"Giske","year":"2015","journal-title":"Clin. Microbiol. Infect."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0185","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S1473-3099(15)00424-7","article-title":"Emergence of plasmid-mediated colistin resistance mechanism MCR-1 in animals and human beings in China: a microbiological and molecular biological study","volume":"16","author":"Liu","year":"2016","journal-title":"Lancet Infect. Dis."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0190","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/S0167-7799(97)01156-6","article-title":"Cationic peptides: a new source of antibiotics","volume":"16","author":"Hancock","year":"1998","journal-title":"Trends Biotechnol."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0195","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1002\/psc.2656","article-title":"On the design of supramolecular assemblies made of peptides and lipid bilayers","volume":"20","author":"Kemayo Koumkoua","year":"2014","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0200","doi-asserted-by":"crossref","first-page":"2665","DOI":"10.1128\/AAC.49.7.2665-2672.2005","article-title":"Antimicrobial activity of novel dendrimeric peptides obtained by phage display selection and rational modification","volume":"49","author":"Pini","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0205","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1002\/psc.858","article-title":"Characterization of the branched antimicrobial peptide M6 by analyzing its mechanism of action and in vivo toxicity","volume":"13","author":"Pini","year":"2007","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0210","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.jinorgbio.2012.03.004","article-title":"The use of a ditopic Gd(III) paramagnetic probe for investigating \u03b1-bungarotoxin surface accessibility","volume":"112","author":"Bernini","year":"2012","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0215","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/j.bbapap.2013.12.012","article-title":"Searching for protein binding sites from molecular dynamics simulations and paramagnetic fragment-based NMR studies","volume":"1844","author":"Bernini","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2017.06.001_bb0220","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.bpc.2008.07.003","article-title":"NMR studies on the surface accessibility of the archaeal protein Sso7d by using TEMPOL and Gd(III)(DTPA-BMA) as paramagnetic probes","volume":"137","author":"Bernini","year":"2008","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0225","doi-asserted-by":"crossref","first-page":"13155","DOI":"10.1073\/pnas.1507893112","article-title":"Helical antimicrobial polypeptides with radial amphiphilicity","volume":"112","author":"Xiong","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0230","doi-asserted-by":"crossref","first-page":"5776","DOI":"10.1021\/ja0584875","article-title":"Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region","volume":"128","author":"Li","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0235","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1034\/j.1399-3011.2002.01968.x","article-title":"Solution structure of a cathelicidin-derived antimicrobial peptide, CRAMP as determined by NMR spectroscopy","volume":"60","author":"Yu","year":"2002","journal-title":"J. Pept. Res."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0240","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1074\/jbc.M406509200","article-title":"Structure-activity relationships of diastereomeric lysine ring size analogs of the antimicrobial peptide gramicidin S: mechanism of action and discrimination between bacterial and animal cell membranes","volume":"280","author":"Prenner","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0245","doi-asserted-by":"crossref","first-page":"366","DOI":"10.3390\/ph7040366","article-title":"\u201cSpecificity determinants\u201d improve therapeutic indices of two antimicrobial peptides piscidin 1 and dermaseptin S4 against the Gram-negative pathogens Acinetobacter baumannii and Pseudomonas aeruginosa","volume":"7","author":"Jiang","year":"2014","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.bbamem.2017.06.001_bb0250","doi-asserted-by":"crossref","first-page":"13301","DOI":"10.1074\/jbc.M116.719575","article-title":"Role of aromatic amino acids in lipopolysaccharide and membrane interactions of antimicrobial peptides for use in plant disease control","volume":"291","author":"Datta","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0255","doi-asserted-by":"crossref","first-page":"11951","DOI":"10.1038\/srep11951","article-title":"Antimicrobial peptides: insights into membrane permeabilization, lipopolysaccharide fragmentation and application in plant disease control","volume":"5","author":"Datta","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0260","doi-asserted-by":"crossref","first-page":"e46259","DOI":"10.1371\/journal.pone.0046259","article-title":"Isomerization of an antimicrobial peptide broadens antimicrobial spectrum to Gram-positive bacterial pathogens","volume":"7","author":"Falciani","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamem.2017.06.001_bb0265","doi-asserted-by":"crossref","first-page":"3132","DOI":"10.1128\/AAC.00124-10","article-title":"Damage of the bacterial cell envelope by antimicrobial peptides gramicidin S and PGLa as revealed by transmission and scanning electron microscopy","volume":"54","author":"Hartmann","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbamem.2017.06.001_bb0270","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1016\/j.bbamem.2006.02.021","article-title":"Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic alpha-helical antimicrobial peptides","volume":"1758","author":"Sato","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2017.06.001_bb0275","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.3390\/ph6121543","article-title":"Antimicrobial peptides","volume":"6","author":"Bahar","year":"2013","journal-title":"Pharmaceuticals"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273617301827?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273617301827?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,9,1]],"date-time":"2018-09-01T00:23:18Z","timestamp":1535761398000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0005273617301827"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,10]]},"references-count":55,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2017,10]]}},"alternative-id":["S0005273617301827"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamem.2017.06.001","relation":{},"ISSN":["0005-2736"],"issn-type":[{"value":"0005-2736","type":"print"}],"subject":[],"published":{"date-parts":[[2017,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Investigations into the killing activity of an antimicrobial peptide active against extensively antibiotic-resistant K. pneumon iae and P. aeruginosa","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Biomembranes","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbamem.2017.06.001","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}