{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,20]],"date-time":"2026-05-20T05:45:15Z","timestamp":1779255915148,"version":"3.51.4"},"reference-count":50,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2016,11,1]],"date-time":"2016-11-01T00:00:00Z","timestamp":1477958400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2016,8,8]],"date-time":"2016-08-08T00:00:00Z","timestamp":1470614400000},"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":[[2016,11]]},"DOI":"10.1016\/j.bbamem.2016.07.018","type":"journal-article","created":{"date-parts":[[2016,7,30]],"date-time":"2016-07-30T21:02:12Z","timestamp":1469912532000},"page":"2737-2744","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":34,"title":["Phospholipid dependent mechanism of smp24, an \u03b1-helical antimicrobial peptide from scorpion venom"],"prefix":"10.1016","volume":"1858","author":[{"given":"Patrick L.","family":"Harrison","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"George R.","family":"Heath","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Benjamin R.G.","family":"Johnson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mohamed A.","family":"Abdel-Rahman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter N.","family":"Strong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephen D.","family":"Evans","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Keith","family":"Miller","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"2","key":"10.1016\/j.bbamem.2016.07.018_bb0005","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.plipres.2011.12.005","article-title":"Role of lipids in the interaction of antimicrobial peptides with membranes","volume":"51","author":"Teixeira","year":"2012","journal-title":"Prog. Lipid Res."},{"issue":"29","key":"10.1016\/j.bbamem.2016.07.018_bb0010","doi-asserted-by":"crossref","first-page":"8347","DOI":"10.1021\/bi000946l","article-title":"Action of antimicrobial peptides: two-state model","volume":"39","author":"Huang","year":"2000","journal-title":"Biochemistry"},{"issue":"1\u20132","key":"10.1016\/j.bbamem.2016.07.018_bb0015","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0005-2736(99)00200-X","article-title":"Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides","volume":"1462","author":"Shai","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"issue":"3","key":"10.1016\/j.bbamem.2016.07.018_bb0020","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":"10.1016\/j.bbamem.2016.07.018_bb0025","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S0033583500000123","article-title":"Electrically gated ionic channels in lipid bilayers","volume":"10","author":"Ehrenstein","year":"1977","journal-title":"Q. Rev. Biophys."},{"issue":"4","key":"10.1016\/j.bbamem.2016.07.018_bb0030","doi-asserted-by":"crossref","first-page":"469","DOI":"10.2165\/00003495-199957040-00002","article-title":"Host defence (cationic) peptides: what is their future clinical potential?","volume":"57","author":"Hancock","year":"1999","journal-title":"Drugs"},{"issue":"5","key":"10.1016\/j.bbamem.2016.07.018_bb0035","first-page":"507","article-title":"Antimicrobial peptides (AMPs): peptide structure and mode of action","volume":"38","author":"Park","year":"2005","journal-title":"J. Biochem. Mol. Biol."},{"issue":"1\u20132","key":"10.1016\/j.bbamem.2016.07.018_bb0040","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.bbamem.2003.08.010","article-title":"The haemolytic activity of six arachnid cationic peptides is affected by the phosphatidylcholine-to-sphingomyelin ratio in lipid bilayers","volume":"1617","author":"Belokoneva","year":"2003","journal-title":"Biochim. Biophys. Acta"},{"issue":"51","key":"10.1016\/j.bbamem.2016.07.018_bb0045","doi-asserted-by":"crossref","first-page":"10124","DOI":"10.1021\/bi3015086","article-title":"Lipid dependence of antimicrobial peptide activity is an unreliable experimental test for different pore models","volume":"51","author":"Bobone","year":"2012","journal-title":"Biochemistry"},{"issue":"4","key":"10.1016\/j.bbamem.2016.07.018_bb0050","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1016\/j.bbamem.2009.07.026","article-title":"Nanoscale analysis of supported lipid bilayers using atomic force microscopy","volume":"1798","author":"El Kirat","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"issue":"6","key":"10.1016\/j.bbamem.2016.07.018_bb0055","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1016\/j.bbamem.2010.11.010","article-title":"Investigating the effects of L- to D-amino acid substitution and deamidation on the activity and membrane interactions of antimicrobial peptide anoplin","volume":"1808","author":"Won","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"issue":"45","key":"10.1016\/j.bbamem.2016.07.018_bb0060","doi-asserted-by":"crossref","first-page":"15739","DOI":"10.1039\/c2cp43099a","article-title":"The antimicrobial peptide aurein 1.2 disrupts model membranes via the carpet mechanism","volume":"14","author":"Fernandez","year":"2012","journal-title":"Phys. Chem. Chem. Phys."},{"issue":"42","key":"10.1016\/j.bbamem.2016.07.018_bb0065","doi-asserted-by":"crossref","first-page":"21282","DOI":"10.1021\/jp0630065","article-title":"Mechanism of supported membrane disruption by antimicrobial peptide protegrin-1","volume":"110","author":"Lam","year":"2007","journal-title":"J. Phys. Chem. B"},{"issue":"2","key":"10.1016\/j.bbamem.2016.07.018_bb0070","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.bbamem.2011.11.002","article-title":"Mechanism of structural transformations induced by antimicrobial peptides in lipid membranes","volume":"1818","author":"Lam","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"issue":"6","key":"10.1016\/j.bbamem.2016.07.018_bb0075","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1016\/j.bbamem.2016.03.002","article-title":"Atomic force microscopy of bacteria reveals the mechanobiology of pore forming peptide action","volume":"1858","author":"Mularski","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0080","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.toxicon.2014.06.006","article-title":"Antimicrobial peptides from scorpion venoms","volume":"88","author":"Harrison","year":"2014","journal-title":"Toxicon"},{"issue":"9","key":"10.1016\/j.bbamem.2016.07.018_bb0085","doi-asserted-by":"crossref","first-page":"2140","DOI":"10.1016\/j.bbamem.2013.10.022","article-title":"Membrane interactions and biological activity of antimicrobial peptides from Australian scorpion","volume":"1838","author":"Luna-Ram\u00edrez","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0090","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.toxicon.2013.08.064","article-title":"Venom proteomic and venomous glands transcriptomic analysis of the Egyptian scorpion Scorpio maurus palmatus (Arachnida: Scorpionidae)","volume":"74","author":"Abdel-Rahman","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0095","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"},{"issue":"10","key":"10.1016\/j.bbamem.2016.07.018_bb0100","doi-asserted-by":"crossref","first-page":"2355","DOI":"10.1016\/j.bpj.2013.10.007","article-title":"Actin assembly at model-supported lipid bilayers","volume":"105","author":"Heath","year":"2013","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2016.07.018_bb0105","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1039\/C2FD20119D","article-title":"Critical point fluctuations in supported lipid membranes","volume":"161","author":"Connell","year":"2013","journal-title":"Faraday Discuss."},{"issue":"1","key":"10.1016\/j.bbamem.2016.07.018_bb0110","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1124\/pr.55.1.2","article-title":"Mechanisms of antimicrobial peptide action and resistance","volume":"55","author":"Yeaman","year":"2003","journal-title":"Pharmacol. Rev."},{"key":"10.1016\/j.bbamem.2016.07.018_bb0115","series-title":"Microbial Lipids","volume":"1","author":"Ratledge","year":"1988"},{"issue":"10","key":"10.1016\/j.bbamem.2016.07.018_bb0120","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"},{"issue":"9049","key":"10.1016\/j.bbamem.2016.07.018_bb0125","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1016\/S0140-6736(97)80051-7","article-title":"Peptide antibiotics","volume":"349","author":"Hancock","year":"1997","journal-title":"Lancet"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0130","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/j.bpj.2012.11.3836","article-title":"Conical lipids in flat bilayers induce packing defects similar to that induced by positive curvature","volume":"104","author":"Vamparys","year":"2013","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2016.07.018_bb0135","doi-asserted-by":"crossref","first-page":"1840","DOI":"10.1016\/j.febslet.2009.10.022","article-title":"Amphipathic helices and membrane curvature","volume":"584","author":"Drin","year":"2010","journal-title":"FEBS Lett."},{"issue":"29","key":"10.1016\/j.bbamem.2016.07.018_bb0140","doi-asserted-by":"crossref","first-page":"20883","DOI":"10.1074\/jbc.M113.478297","article-title":"\u03b1-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling","volume":"288","author":"Ouberai","year":"2013","journal-title":"J. Biol. Chem."},{"issue":"49","key":"10.1016\/j.bbamem.2016.07.018_bb0145","doi-asserted-by":"crossref","first-page":"18149","DOI":"10.1523\/JNEUROSCI.4345-11.2011","article-title":"Synapsin I senses membrane curvature by an amphipathic lipid packing sensor motif","volume":"31","author":"Krabben","year":"2011","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbamem.2016.07.018_bb0150","doi-asserted-by":"crossref","first-page":"2244","DOI":"10.1038\/sj.emboj.7600714","article-title":"ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif","volume":"24","author":"Bigay","year":"2004","journal-title":"EMBO J."},{"key":"10.1016\/j.bbamem.2016.07.018_bb0155","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1146\/annurev-biochem-052809-155121","article-title":"Mechanisms of membrane curvature sensing","volume":"80","author":"Antonny","year":"2011","journal-title":"Annu. Rev. Biochem."},{"issue":"70","key":"10.1016\/j.bbamem.2016.07.018_bb0160","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"},{"issue":"4","key":"10.1016\/j.bbamem.2016.07.018_bb0165","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1007\/s00249-010-0652-5","article-title":"QCM-D fingerprinting of membrane-active peptides","volume":"40","author":"McCubbin","year":"2011","journal-title":"Eur. Biophys. J."},{"issue":"1","key":"10.1016\/j.bbamem.2016.07.018_bb0170","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1529\/biophysj.106.100370","article-title":"Pore formation by a Bax-derived peptide: effect on the line tension of the membrane probed by AFM","volume":"93","author":"Garc\u00eda-S\u00e1ez","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2016.07.018_bb0175","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.chemphyslip.2009.09.002","article-title":"Induction of non-lamellar lipid phases by antimicrobial peptides: a potential link to mode of action","volume":"163","author":"Haney","year":"2010","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0180","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/1757-5036-2-3","article-title":"The multiple faces of self-assembled lipidic systems","volume":"2","author":"Tresset","year":"2009","journal-title":"PMC Biophys."},{"key":"10.1016\/j.bbamem.2016.07.018_bb0185","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/S0006-3495(97)78064-0","article-title":"Effect of changing the size of lipid headgroup on peptide insertion into membranes","volume":"73","author":"Heller","year":"1997","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2016.07.018_bb0190","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/S0009-3084(01)00157-8","article-title":"Packing characteristics of a model system mimicking cytoplasmic bacterial membranes","volume":"111","author":"Lohner","year":"2001","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0195","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.bbamem.2005.08.003","article-title":"Composition dependence of vesicle morphology and mixing properties in a bacterial model membrane system","volume":"1716","author":"Pozo Navas","year":"2005","journal-title":"Biochim. Biophys. Acta (BBA)"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0200","doi-asserted-by":"crossref","first-page":"14346","DOI":"10.1021\/ja8062327","article-title":"Bacterial membranes as predictors of antimicrobial potency","volume":"130","author":"Epand","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbamem.2016.07.018_bb0205","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/S0304-4157(98)00015-X","article-title":"Lipid polymorphism and protein-lipid interactions","volume":"1376","author":"Epand","year":"1998","journal-title":"Biochim. Biophys. Acta Rev. Biomembr."},{"key":"10.1016\/j.bbamem.2016.07.018_bb0210","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/S0005-2736(99)00207-2","article-title":"The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes","volume":"1462","author":"Prenner","year":"1999","journal-title":"Biochim. Biophys. Acta (BBA)"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0215","doi-asserted-by":"crossref","first-page":"7906","DOI":"10.1021\/bi962785k","article-title":"Nonlamellar phases induced by the interaction of gramicidin S with lipid bilayers. A possible relationship to membrane-disrupting activity","volume":"36","author":"Prenner","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0220","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/j.bbrc.2008.01.176","article-title":"Membrane curvature stress and antibacterial activity of lactoferricin derivatives","volume":"369","author":"Zweytick","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamem.2016.07.018_bb0225","doi-asserted-by":"crossref","first-page":"2325","DOI":"10.1016\/j.bbamem.2008.05.014","article-title":"Influence of antimicrobial peptides on the formation of nonlamellar lipid mesophases","volume":"1778","author":"Hickel","year":"2008","journal-title":"Biochim. Biophys. Acta (BBA)"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0230","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/0005-2736(95)00229-4","article-title":"Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures","volume":"1278","author":"Keller","year":"1996","journal-title":"Biochim. Biophys. Acta (BBA)"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0235","first-page":"650","article-title":"Peptide induced demixing in PG\/PE lipid mixtures: a mechanism for the specificity of antimicrobial peptides towards bacterial membranes?","author":"Arouri","year":"1788","journal-title":"Biochim Biophys Acta (BBA)"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0240","doi-asserted-by":"crossref","first-page":"16198","DOI":"10.1021\/jp106915c","article-title":"Influence of lysine Ne-trimethylation and lipid composition on the membrane activity of the cecropin A-melittin hybrid peptide CA(1\u20137)M(2\u20139)","volume":"114","author":"Teixeira","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbamem.2016.07.018_bb0245","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.bbamem.2008.08.023","article-title":"Lipid domains in bacterial membranes and the action of antimicrobial agents","volume":"1788","author":"Epand","year":"2009","journal-title":"Biochim. Biophys. Acta (BBA)"},{"issue":"17","key":"10.1016\/j.bbamem.2016.07.018_bb0250","doi-asserted-by":"crossref","first-page":"11584","DOI":"10.1074\/jbc.M114.554444","article-title":"Cardiolipin prevents membrane translocation and permeabilization by daptomycin. 2014","volume":"289","author":"Zhang","year":"2014","journal-title":"J. Biol. Chem."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273616302711?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273616302711?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,7,13]],"date-time":"2018-07-13T15:15:01Z","timestamp":1531494901000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0005273616302711"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,11]]},"references-count":50,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2016,11]]}},"alternative-id":["S0005273616302711"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamem.2016.07.018","relation":{},"ISSN":["0005-2736"],"issn-type":[{"value":"0005-2736","type":"print"}],"subject":[],"published":{"date-parts":[[2016,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Phospholipid dependent mechanism of smp24, an \u03b1-helical antimicrobial peptide from scorpion venom","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.2016.07.018","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}