Interaction of cationic antimicrobial peptides with Mycoplasma pulmonis
DC Field | Value | Language |
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dc.contributor.author | Park, Ho Jin | - |
dc.contributor.author | Kang, Ki Mo | - |
dc.contributor.author | Dybvig, Kevin | - |
dc.contributor.author | Lee, Bok Luel | - |
dc.contributor.author | Jung, Yong Woo | - |
dc.contributor.author | Lee, In Hee | - |
dc.date.accessioned | 2021-09-05T20:13:59Z | - |
dc.date.available | 2021-09-05T20:13:59Z | - |
dc.date.created | 2021-06-15 | - |
dc.date.issued | 2013-10-11 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/101877 | - |
dc.description.abstract | We investigated the mode of action underlying the anti-mycoplasma activity of cationic antimicrobial peptides (AMPs) using four known AMPs and Mycoplasma pulmonis as a model mycoplasma. Scanning electron microscopy revealed that the integrity of the M. pulmonis membrane was significantly damaged within 30 min of AMPs exposure, which was confirmed by measuring the uptake of propidium iodine into the mycoplasma cells. The anti-mycoplasma activity of AMPs was found to depend on the binding affinity for phosphatidylcholine, which was incorporated into the mycoplasma membrane from the growth medium and preferentially distributed in the outer leaflet of the lipid bilayer. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | WILEY | - |
dc.subject | MEMBRANES | - |
dc.title | Interaction of cationic antimicrobial peptides with Mycoplasma pulmonis | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Jung, Yong Woo | - |
dc.identifier.doi | 10.1016/j.febslet.2013.08.016 | - |
dc.identifier.scopusid | 2-s2.0-84884908352 | - |
dc.identifier.wosid | 000325078600006 | - |
dc.identifier.bibliographicCitation | FEBS LETTERS, v.587, no.20, pp.3321 - 3326 | - |
dc.relation.isPartOf | FEBS LETTERS | - |
dc.citation.title | FEBS LETTERS | - |
dc.citation.volume | 587 | - |
dc.citation.number | 20 | - |
dc.citation.startPage | 3321 | - |
dc.citation.endPage | 3326 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | MEMBRANES | - |
dc.subject.keywordAuthor | Antimicrobial peptide | - |
dc.subject.keywordAuthor | Mycoplasma | - |
dc.subject.keywordAuthor | Phospholipid | - |
dc.subject.keywordAuthor | Liposome | - |
dc.subject.keywordAuthor | Action mechanism | - |
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