{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,25]],"date-time":"2026-03-25T19:05:45Z","timestamp":1774465545746,"version":"3.50.1"},"reference-count":43,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2014,2,1]],"date-time":"2014-02-01T00:00:00Z","timestamp":1391212800000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea (NRF)","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Korea government (MEST)","award":["No. 2011\u20100017532"],"award-info":[{"award-number":["No. 2011\u20100017532"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"published-print":{"date-parts":[[2013,2]]},"DOI":"10.1016\/j.bbamem.2012.09.005","type":"journal-article","created":{"date-parts":[[2012,9,13]],"date-time":"2012-09-13T15:26:10Z","timestamp":1347549970000},"page":"443-454","source":"Crossref","is-referenced-by-count":57,"title":["Antimicrobial HPA3NT3 peptide analogs: Placement of aromatic rings and positive charges are key determinants for cell selectivity and mechanism of action"],"prefix":"10.1016","volume":"1828","author":[{"given":"Jong-Kook","family":"Lee","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Seong-Cheol","family":"Park","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kyung-Soo","family":"Hahm","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yoonkyung","family":"Park","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamem.2012.09.005_bb0005","first-page":"238","article-title":"Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?","volume":"3","author":"Brogden","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.bbamem.2012.09.005_bb0010","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":"10.1016\/j.bbamem.2012.09.005_bb0015","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.2012.09.005_bb0020","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.1084\/jem.191.9.1451","article-title":"Modulating phagocyte activation: the pros and cons of Helicobacter pylori virulence factors","volume":"191","author":"Allen","year":"2000","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0025","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/19439","article-title":"Antibacterial peptide from H. pylori","volume":"398","author":"P\u00fctsep","year":"1999","journal-title":"Nature"},{"key":"10.1016\/j.bbamem.2012.09.005_bb0030","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1128\/AAC.45.6.1700-1704.2001","article-title":"Proinflammatory activity of a cecropin-like antibacterial peptide from Helicobacter pylori","volume":"45","author":"Bylund","year":"2001","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0035","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.bbamem.2007.09.020","article-title":"Amphipathic alpha-helical peptide, HP (2\u201020), and its analogues derived from Helicobacter pylori: pore formation mechanism in various lipid compositions","volume":"1778","author":"Park","year":"2008","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0040","doi-asserted-by":"crossref","first-page":"31609","DOI":"10.1074\/jbc.272.50.31609","article-title":"Selective cytotoxicity of dermaseptin S3 toward intraerythrocytic Plasmodium falciparum and the underlying molecular basis","volume":"272","author":"Ghosh","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0045","doi-asserted-by":"crossref","first-page":"6502","DOI":"10.1016\/S0021-9258(19)50456-2","article-title":"Aggregation and organization of pardaxin in phospholipid membranes","volume":"267","author":"Rapaport","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0050","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1016\/j.bbrc.2007.07.188","article-title":"Characterization of a heat-stable protein with antimicrobial activity from Arabidopsis thaliana","volume":"362","author":"Park","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0055","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1002\/bip.20679","article-title":"Structure-activity relationship of HP (2\u201020) analog peptide: enhanced antimicrobial activity by N-terminal random coil region deletion","volume":"88","author":"Park","year":"2007","journal-title":"Biopolymers"},{"key":"10.1016\/j.bbamem.2012.09.005_bb0060","doi-asserted-by":"crossref","first-page":"3350","DOI":"10.1021\/bi00713a027","article-title":"Determination of the helix and beta form of proteins in aqueous solution by circular dichroism","volume":"13","author":"Chen","year":"1974","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2012.09.005_bb0065","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.chembiol.2006.11.009","article-title":"In vitro discriminative antipseudomonal properties resulting from acyl substitution of N-terminal sequence of dermaseptin S4 derivatives","volume":"14","author":"Marynka","year":"2007","journal-title":"Chem. Biol."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0070","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1042\/bj20031975","article-title":"Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability and viability of Escherichia coli","volume":"380","author":"Mangoni","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0075","doi-asserted-by":"crossref","first-page":"5277","DOI":"10.1021\/jf070108z","article-title":"Purification and characterization of an antifungal protein, C-FKBP, from Chinese cabbage","volume":"55","author":"Park","year":"2007","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0080","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/S0167-4838(02)00373-4","article-title":"Design of novel analogue peptides with potent antibiotic activity based on the antimicrobial peptide, HP (2\u201020), derived from N-terminus of Helicobacter pylori ribosomal protein L1","volume":"1598","author":"Lee","year":"2002","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2012.09.005_bb0085","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/0005-2736(86)90302-0","article-title":"Vesicles of variable sizes produced by a rapid extrusion procedure","volume":"858","author":"Mayer","year":"1986","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2012.09.005_bb0090","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/0003-2697(80)90269-9","article-title":"Colorimetric determination of phospholipids with ammonium ferrothiocyanate","volume":"104","author":"Stewart","year":"1980","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0095","doi-asserted-by":"crossref","first-page":"27182","DOI":"10.1074\/jbc.273.42.27182","article-title":"Serum-induced leakage of liposome contents","volume":"273","author":"Ghosh","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0100","doi-asserted-by":"crossref","first-page":"4053","DOI":"10.1093\/nar\/gki725","article-title":"Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA","volume":"33","author":"Hsu","year":"2005","journal-title":"Nucleic Acids Res."},{"issue":"14","key":"10.1016\/j.bbamem.2012.09.005_bb0105","doi-asserted-by":"crossref","first-page":"5978","DOI":"10.1073\/pnas.0811231106","article-title":"Heat-shock dependent oligomeric status alters the function of a plant-specific thioredoxin-like protein, AtTDX","volume":"106","author":"Lee","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0110","doi-asserted-by":"crossref","first-page":"3302","DOI":"10.1128\/AAC.49.8.3302-3310.2005","article-title":"Systemic antibacterial activity of novel synthetic cyclic peptides","volume":"49","author":"Dartois","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"issue":"4","key":"10.1016\/j.bbamem.2012.09.005_bb0220","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1111\/j.1751-1097.1973.tb06422.x","article-title":"Fluorescence and the location of tryptophan residues in protein molecules","volume":"18","author":"Burstein","year":"1973","journal-title":"Photochem. Photobiol."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0120","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."},{"issue":"5","key":"10.1016\/j.bbamem.2012.09.005_bb0125","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.1093\/emboj\/20.5.1164","article-title":"Mutations in DnaA protein suppress the growth arrest of acidic phospholipid-deficient Escherichia coli cells","volume":"20","author":"Zheng","year":"2001","journal-title":"EMBO J."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0130","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1016\/S0006-3495(01)75802-X","article-title":"Barrel-stave model or toroidal model? A case study on melittin pores","volume":"81","author":"Yang","year":"2001","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0135","doi-asserted-by":"crossref","first-page":"2520","DOI":"10.1016\/S0006-3495(02)75595-1","article-title":"Size distribution of barrel-stave aggregates of membrane peptides: influence of the bilayer lateral pressure profile","volume":"82","author":"Cantor","year":"2002","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0140","doi-asserted-by":"crossref","first-page":"10681","DOI":"10.1021\/bi00201a016","article-title":"Mode of action of the antibacterial cecropin B2: a spectrofluorometric study","volume":"33","author":"Gazit","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2012.09.005_bb0145","doi-asserted-by":"crossref","first-page":"1762","DOI":"10.1016\/S0006-3495(97)78822-2","article-title":"Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: pore formation by melittin","volume":"72","author":"Ladokhin","year":"1997","journal-title":"Biophys. J."},{"issue":"2","key":"10.1016\/j.bbamem.2012.09.005_bb0150","doi-asserted-by":"crossref","first-page":"1310","DOI":"10.1074\/jbc.M208762200","article-title":"Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes","volume":"278","author":"Takeshima","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0155","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/S0968-0004(00)01626-1","article-title":"How proteins adapt to a membrane-water interface","volume":"25","author":"Killian","year":"2000","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0160","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1002\/pro.5560060407","article-title":"Architecture of helix bundle membrane proteins: an analysis of cytochrome c oxidase from bovine mitochondria","volume":"6","author":"Wallin","year":"1997","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0165","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1002\/prot.340080202","article-title":"Amphipathic helix motif: classes and properties","volume":"8","author":"Segrest","year":"1990","journal-title":"Proteins"},{"key":"10.1016\/j.bbamem.2012.09.005_bb0170","doi-asserted-by":"crossref","first-page":"20839","DOI":"10.1074\/jbc.274.30.20839","article-title":"Different membrane anchoring positions of tryptophan and lysine in synthetic transmembrane alpha-helical peptides","volume":"274","author":"de Planque","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0175","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1074\/jbc.M111.279281","article-title":"Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity","volume":"287","author":"Rekdal","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0180","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/S0005-2736(99)00201-1","article-title":"Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells","volume":"1462","author":"Dathe","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2012.09.005_bb0185","doi-asserted-by":"crossref","first-page":"5589","DOI":"10.1046\/j.1432-1033.2001.02494.x","article-title":"Amphipathic alpha helical antimicrobial peptides","volume":"268","author":"Giangaspero","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0190","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1139\/o02-147","article-title":"Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions","volume":"80","author":"Schibli","year":"2002","journal-title":"Biochem. Cell Biol."},{"issue":"5","key":"10.1016\/j.bbamem.2012.09.005_bb0195","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1002\/psc.1369","article-title":"Reversed sequence enhances antimicrobial activity of a synthetic peptide","volume":"17","author":"Gopal","year":"2011","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.bbamem.2012.09.005_bb0200","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."},{"issue":"2","key":"10.1016\/j.bbamem.2012.09.005_bb0205","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/S1570-9639(02)00541-1","article-title":"A Leu-Lys-rich antimicrobial peptide: activity and mechanism","volume":"1645","author":"Park","year":"2003","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2012.09.005_bb0210","doi-asserted-by":"crossref","first-page":"2998","DOI":"10.1021\/bi00126a022","article-title":"Binding of tachyplesin I to DNA revealed by footprinting analysis: significant contribution of secondary structure to DNA binding and implication for biological action","volume":"31","author":"Yonezawa","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2012.09.005_bb0215","first-page":"377","article-title":"Lactoferricin B inhibits bacterial macromolecular synthesis in Escherichia coli and Bacillus subtilis","volume":"237","author":"Ulvatne","year":"2004","journal-title":"FEMS Microbiol. Lett."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273612003185?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273612003185?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,1,28]],"date-time":"2022-01-28T22:11:34Z","timestamp":1643407894000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0005273612003185"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,2]]},"references-count":43,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2013,2]]}},"alternative-id":["S0005273612003185"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamem.2012.09.005","relation":{},"ISSN":["0005-2736"],"issn-type":[{"value":"0005-2736","type":"print"}],"subject":[],"published":{"date-parts":[[2013,2]]}}}