Analysis of the solution structure of the human antibiotic peptide dermcidin and its interaction with phospholipid vesicles
DC Field | Value | Language |
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dc.contributor.author | Jung, Hyun Ho | - |
dc.contributor.author | Yang, Sung-Tae | - |
dc.contributor.author | Sim, Ji-Yeong | - |
dc.contributor.author | Lee, Seungkyu | - |
dc.contributor.author | Lee, Ju Yeon | - |
dc.contributor.author | Kim, Ha Hyung | - |
dc.contributor.author | Shin, Song Yub | - |
dc.contributor.author | Kim, Jae Il | - |
dc.date.available | 2019-05-30T01:35:51Z | - |
dc.date.issued | 2010-05-31 | - |
dc.identifier.issn | 1976-6696 | - |
dc.identifier.issn | 1976-670X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/22448 | - |
dc.description.abstract | Dermcidin is a human antibiotic peptide that is secreted by the sweat glands and has no homology to other known antimicrobial peptides. As an initial step toward understanding dermcidin's mode of action at bacterial membranes, we used homonuclear and heteronuclear NMR to determine the conformation of the peptide in 50 h trifluoroethanol solution. We found that dermcidin adopts a flexible amphipathic alpha-helical structure with a helix-hinge-helix motif, which is a common molecular fold among antimicrobial peptides. Spin-down assays of dermcidin and several related peptides revealed that the affinity with which dermcidin binds to bacterial-mimetic membranes is primarily dependent on its amphipathic alpha-helical structure and its length (>30 residues); its negative net charge and acidic pl have little effect on binding. These findings suggest that the mode of action of dermcidin is similar to that of other membrane-targeting antimicrobial peptides, though the details of its antimicrobial action remain to be determined [BMB reports 2010; 43(5): 362-368] | - |
dc.format.extent | 7 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY | - |
dc.title | Analysis of the solution structure of the human antibiotic peptide dermcidin and its interaction with phospholipid vesicles | - |
dc.type | Article | - |
dc.identifier.doi | 10.5483/BMBRep.2010.43.5.362 | - |
dc.identifier.bibliographicCitation | BMB REPORTS, v.43, no.5, pp 362 - 368 | - |
dc.identifier.kciid | ART001445632 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000278244700010 | - |
dc.identifier.scopusid | 2-s2.0-77953488183 | - |
dc.citation.endPage | 368 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 362 | - |
dc.citation.title | BMB REPORTS | - |
dc.citation.volume | 43 | - |
dc.type.docType | Article | - |
dc.publisher.location | 대한민국 | - |
dc.subject.keywordAuthor | Amphipthic alpha-helical structure | - |
dc.subject.keywordAuthor | Antimicrobial peptide | - |
dc.subject.keywordAuthor | Helix-hinge-helix motif | - |
dc.subject.keywordAuthor | Nuclear magnetic resonance (NMR) spectroscopy | - |
dc.subject.keywordAuthor | Peptide-membrane interaction | - |
dc.subject.keywordPlus | HELICAL ANTIMICROBIAL PEPTIDES | - |
dc.subject.keywordPlus | NUCLEAR-MAGNETIC-RESONANCE | - |
dc.subject.keywordPlus | MODEL | - |
dc.subject.keywordPlus | VERTEBRATES | - |
dc.subject.keywordPlus | MEMBRANES | - |
dc.subject.keywordPlus | PORES | - |
dc.subject.keywordPlus | HINGE | - |
dc.subject.keywordPlus | SWEAT | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
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