{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,14]],"date-time":"2026-07-14T14:10:14Z","timestamp":1784038214533,"version":"3.55.0"},"reference-count":49,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2005,3,1]],"date-time":"2005-03-01T00:00:00Z","timestamp":1109635200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Peptides"],"published-print":{"date-parts":[[2005,3]]},"DOI":"10.1016\/j.peptides.2004.10.004","type":"journal-article","created":{"date-parts":[[2004,12,15]],"date-time":"2004-12-15T18:47:39Z","timestamp":1103136459000},"page":"369-375","source":"Crossref","is-referenced-by-count":29,"title":["Deletion of two C-terminal Gln residues of 12\u201326-residue fragment of melittin improves its antimicrobial activity"],"prefix":"10.1016","volume":"26","author":[{"given":"Xuejun","family":"Sun","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suxia","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shunzi","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Husheng","family":"Yan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yunge","family":"Fan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huaifeng","family":"Mi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.peptides.2004.10.004_bib1","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/S0021-9258(18)70226-3","article-title":"Phosphorus assay in column chromatography","volume":"234","author":"Bartlett","year":"1959","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2004.10.004_bib2","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1111\/j.1432-1033.1988.tb13977.x","article-title":"The structure of melittin a 1H-NMR study in methanol","volume":"173","author":"Bazzo","year":"1988","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.peptides.2004.10.004_bib3","doi-asserted-by":"crossref","first-page":"4671","DOI":"10.1021\/bi00233a006","article-title":"Hemolytic and antimicrobial activities of the twenty-four individual omission analogues of melittin","volume":"30","author":"Blondelle","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2004.10.004_bib4","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0145-305X(99)00015-4","article-title":"Antimicrobial peptides in insects; structure and function","volume":"23","author":"Bulet","year":"1999","journal-title":"Dev Comp Immunol"},{"key":"10.1016\/j.peptides.2004.10.004_bib5","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1016\/0014-5793(88)80077-2","article-title":"Synthetic magainin analogues with improved antimicrobial activity","volume":"236","author":"Chen","year":"1988","journal-title":"FEBS Lett"},{"key":"10.1016\/j.peptides.2004.10.004_bib6","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.peptides.2004.10.004_bib7","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.peptides.2004.10.004_bib8","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/0304-4157(90)90006-X","article-title":"The actions of melittin on membrances","volume":"1031","author":"Dempsey","year":"1990","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.peptides.2004.10.004_bib9","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1146\/annurev.bi.53.070184.003115","article-title":"Three-dimensional structure of membrane and surface proteins","volume":"53","author":"Eisenberg","year":"1984","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.peptides.2004.10.004_bib10","doi-asserted-by":"crossref","first-page":"4230","DOI":"10.1074\/jbc.275.6.4230","article-title":"SAR study of antimicrobial dermaseptin S4 showing the consequences of peptide oligomerization on selective cytotoxicity","volume":"275","author":"Feder","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2004.10.004_bib11","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1016\/S1357-4310(99)01490-2","article-title":"Antibiotic peptides from higher eukaryotes: biology and applications","volume":"5","author":"Ganz","year":"1999","journal-title":"Mol Med Today"},{"key":"10.1016\/j.peptides.2004.10.004_bib12","doi-asserted-by":"crossref","first-page":"11479","DOI":"10.1021\/bi00036a021","article-title":"Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles","volume":"34","author":"Gazit","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2004.10.004_bib13","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1021\/bi00118a014","article-title":"Mechanism of the conformational transition of melittin","volume":"31","author":"Goto","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2004.10.004_bib14","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 defenses","volume":"8","author":"Hancock","year":"2000","journal-title":"Trends Microbiol"},{"key":"10.1016\/j.peptides.2004.10.004_bib15","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1303\/aez.31.465","article-title":"Effect of moricin, a novel antibacterial peptide of Bombyx mori (Lepidoptera bombycidae) on the growth of methicillin-resistant Staphylococcus aureus (MRSA)","volume":"31","author":"Hara","year":"1996","journal-title":"Appl Entomol Zool"},{"key":"10.1016\/j.peptides.2004.10.004_bib16","doi-asserted-by":"crossref","first-page":"5985","DOI":"10.1021\/bi00440a040","article-title":"Structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by two-dimensional NMR and distance geometry calculations","volume":"28","author":"Inagaki","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2004.10.004_bib17","doi-asserted-by":"crossref","first-page":"8989","DOI":"10.1021\/ja9542911","article-title":"Synthetic melittin, its enantio, retro, and retroenantio isomers, and selected chimeric analogs: their antibacterial, hemolytic, and lipid bilayer action","volume":"118","author":"Juvvadi","year":"1996","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.peptides.2004.10.004_bib18","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/1380-2933(95)00006-2","article-title":"Antimicrobial activity of human CAP18 peptides","volume":"1","author":"Larrick","year":"1995","journal-title":"Immunotechnology"},{"key":"10.1016\/j.peptides.2004.10.004_bib19","first-page":"449","article-title":"Studies on synthesis and biological activities of analogues of melittin","volume":"24","author":"Li","year":"2003","journal-title":"Chem J Chin Univ"},{"key":"10.1016\/j.peptides.2004.10.004_bib20","series-title":"Peptides: biology and chemistry","article-title":"Hemolytic and antibacterial activity of synthetic deletion peptides of melittin","author":"Liu","year":"1995"},{"key":"10.1016\/j.peptides.2004.10.004_bib21","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1111\/j.1399-3011.1994.tb00381.x","article-title":"Interaction of calmodulin with synthetic deletion peptides of melittin","volume":"43","author":"Liu","year":"1994","journal-title":"Int J Pept Protein Res"},{"key":"10.1016\/j.peptides.2004.10.004_bib22","doi-asserted-by":"crossref","first-page":"12466","DOI":"10.1073\/pnas.92.26.12466","article-title":"Inhibition of a plant virus infection by analogs of melittin","volume":"92","author":"Macros","year":"1995","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.peptides.2004.10.004_bib23","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0005-2736(99)00197-2","article-title":"Why and how are peptide\u2013lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes","volume":"1462","author":"Matsuzaki","year":"1999","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.peptides.2004.10.004_bib24","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1006\/bbrc.1996.0438","article-title":"Isolation and characterization of a new member of insect defensin family from a beetle Allomyrina dichotoma","volume":"220","author":"Miyanoshita","year":"1996","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.peptides.2004.10.004_bib25","doi-asserted-by":"crossref","first-page":"1934","DOI":"10.1016\/S0021-9258(17)42116-8","article-title":"The NH2-terminal helical domain 1\u201318 of dermaseptin is responsible for antimicrobial activity","volume":"269","author":"Mor","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2004.10.004_bib26","doi-asserted-by":"crossref","first-page":"23296","DOI":"10.1074\/jbc.274.33.23296","article-title":"Structure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin","volume":"274","author":"Nagpal","year":"1999","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2004.10.004_bib27","doi-asserted-by":"crossref","first-page":"1064","DOI":"10.1126\/science.257.5073.1064","article-title":"The crisis in antibiotic resistance","volume":"257","author":"Neu","year":"1992","journal-title":"Science"},{"key":"10.1016\/j.peptides.2004.10.004_bib28","doi-asserted-by":"crossref","first-page":"9438","DOI":"10.1021\/bi00198a009","article-title":"Vesicle-bound conformation of melittin: transferred nuclear overhauser enhancement analysis in the presence of perdeuterated phosphatidylcholinevesiclest","volume":"33","author":"Okada","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2004.10.004_bib29","doi-asserted-by":"crossref","first-page":"1826","DOI":"10.1021\/bi962507l","article-title":"Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study","volume":"36","author":"Oren","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2004.10.004_bib30","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1006\/bbrc.1996.0783","article-title":"Identification and isolation of the bactericidal domains in the proteinase inhibitor aprotinin","volume":"222","author":"Pellegrini","year":"1996","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.peptides.2004.10.004_bib31","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1042\/bj2990587","article-title":"Determination of the secondary structure of selected melittin analogues with different hemolytic activities","volume":"299","author":"Perez-Paya","year":"1994","journal-title":"Biochem J"},{"key":"10.1016\/j.peptides.2004.10.004_bib32","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1074\/jbc.270.3.1048","article-title":"The role of amphipathicity in the folding, self-association and biological activity of multiple subunit small proteins","volume":"270","author":"Perez-Paya","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2004.10.004_bib33","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1002\/(SICI)1099-1387(199901)5:1<32::AID-PSC172>3.0.CO;2-9","article-title":"Construction and synthesis of lactoferricin derivatives with enhanced antibacterial activity","volume":"5","author":"Rekdal","year":"1999","journal-title":"J Pept Sci"},{"key":"10.1016\/j.peptides.2004.10.004_bib34","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1042\/bj3160525","article-title":"Dimerization of truncated melittin analogues results in cytolytic peptides","volume":"316","author":"Revitt","year":"1996","journal-title":"Biochem J"},{"key":"10.1016\/j.peptides.2004.10.004_bib35","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1128\/AAC.45.5.1367-1373.2001","article-title":"Anticandida activity is retained in P-113, a 12-amino-acid fragment of histatin 5","volume":"45","author":"Rothstein","year":"2001","journal-title":"Antimicrob Agents Chemother"},{"key":"10.1016\/j.peptides.2004.10.004_bib36","doi-asserted-by":"crossref","first-page":"10697","DOI":"10.1021\/ja00053a003","article-title":"Partitioning of free energy contributions in the estimation of binding constants: residual motion and consequences for amide\u2013amide hydrogen bond strengths","volume":"114","author":"Searle","year":"1992","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.peptides.2004.10.004_bib37","doi-asserted-by":"crossref","first-page":"1629","DOI":"10.1016\/S0196-9781(01)00498-3","article-title":"From \u201ccarpet\u201d mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides","volume":"22","author":"Shai","year":"2001","journal-title":"Peptides"},{"key":"10.1016\/j.peptides.2004.10.004_bib38","doi-asserted-by":"crossref","first-page":"1738","DOI":"10.1128\/AAC.41.8.1738","article-title":"Protegrin-l: a broad-spectrum, rapidly microbicidal peptide with in vivo activity","volume":"41","author":"Steinberg","year":"1997","journal-title":"Antimicrob Agents Chemother"},{"key":"10.1016\/j.peptides.2004.10.004_bib39","doi-asserted-by":"crossref","first-page":"6016","DOI":"10.1016\/S0021-9258(20)65098-0","article-title":"The structure of melittin II Interpretation of the structure","volume":"257","author":"Terwilliger","year":"1982","journal-title":"J Biol Chem"},{"key":"10.1016\/j.peptides.2004.10.004_bib40","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1093\/protein\/9.12.1219","article-title":"Specific antimicrobial and hemolytic activities of 18-residue peptides derived from the amino terminal region of the toxin pardaxin","volume":"9","author":"Thennarasu","year":"1996","journal-title":"Protein Eng"},{"key":"10.1016\/j.peptides.2004.10.004_bib41","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1002\/1097-0282(2000)55:1<4::AID-BIP30>3.0.CO;2-M","article-title":"Amphipathic \u03b1-helical antimicrobial peptides","volume":"55","author":"Tossi","year":"2000","journal-title":"Biopolymers"},{"key":"10.1016\/j.peptides.2004.10.004_bib42","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1126\/science.8153615","article-title":"Reviving the antibiotic miracle","volume":"264","author":"Travis","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.peptides.2004.10.004_bib43","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1042\/bj2910275","article-title":"Purification, sequence and antibacterial activity of two novel sapecin homologues from sacrophaga embryonic cells: similarity of sapecin B to charybdotoxin","volume":"291","author":"Yamada","year":"1993","journal-title":"Biochim J"},{"key":"10.1016\/j.peptides.2004.10.004_bib44","first-page":"295","article-title":"The effect of the basicity and hydrophobicity of peptides on their affinities for calmodulin","volume":"24","author":"Yan","year":"1992","journal-title":"Chin J Biochem Biophys"},{"key":"10.1016\/j.peptides.2004.10.004_bib45","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/S0014-5793(03)01113-X","article-title":"Individual substitution analogs of Mel(12\u201326), melittin's C-terminal 15-residue peptide: their antimicrobial and hemolytic actions","volume":"554","author":"Yan","year":"2003","journal-title":"FEBS Lett"},{"key":"10.1016\/j.peptides.2004.10.004_bib46","first-page":"113","article-title":"Prediction of affinities of peptides for calmodulin","volume":"39","author":"Yan","year":"1996","journal-title":"Sci. China Ser B"},{"key":"10.1016\/j.peptides.2004.10.004_bib47","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1006\/jmbi.1996.0339","article-title":"A microscopic view of helix propagation: N- and C-terminal helix growth in alanine helices","volume":"259","author":"Young","year":"1996","journal-title":"J Mol Biol"},{"key":"10.1016\/j.peptides.2004.10.004_bib48","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/415389a","article-title":"Antimicrobial peptides of multicelullar organisms","volume":"415","author":"Zasloff","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.peptides.2004.10.004_bib49","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1063\/1.1730390","article-title":"Theory of phase transition between helix and random coil in polypeptide chains","volume":"31","author":"Zimm","year":"1959","journal-title":"J Chem Phys"}],"container-title":["Peptides"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0196978104004516?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0196978104004516?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,7,1]],"date-time":"2021-07-01T13:08:17Z","timestamp":1625144897000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0196978104004516"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,3]]},"references-count":49,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2005,3]]}},"alternative-id":["S0196978104004516"],"URL":"https:\/\/doi.org\/10.1016\/j.peptides.2004.10.004","relation":{},"ISSN":["0196-9781"],"issn-type":[{"value":"0196-9781","type":"print"}],"subject":[],"published":{"date-parts":[[2005,3]]}}}