The D-enantiomer of the antimicrobial peptide KLKLLLLLKLK-NH2 preferentially binds to lipopolysaccharide assemblies stabilized by divalent cations.
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| Title: | The D-enantiomer of the antimicrobial peptide KLKLLLLLKLK-NH |
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| Authors: | Sato S; Faculty of Pharmaceutical Sciences, Doshisha Women's College of Liberal Arts, Kyotanabe, Kyoto, 610-0395, Japan., Kawasaki K; Faculty of Pharmaceutical Sciences, Doshisha Women's College of Liberal Arts, Kyotanabe, Kyoto, 610-0395, Japan. Electronic address: kkawasak@dwc.doshisha.ac.jp. |
| Source: | Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2026 Sep 03; Vol. 829, pp. 154186. Date of Electronic Publication: 2026 Jun 22. |
| Publication Type: | Journal Article |
| Journal Info: | Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1090-2104 (Electronic) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE |
| Database: | MEDLINE Ultimate |
| FullText | Text: Availability: 0 |
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| Header | DbId: mdl DbLabel: MEDLINE Ultimate An: 42341419 AccessLevel: 2 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: The D-enantiomer of the antimicrobial peptide KLKLLLLLKLK-NH<subscript>2</subscript> preferentially binds to lipopolysaccharide assemblies stabilized by divalent cations. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AU" term="%22Sato+S%22">Sato S</searchLink>; Faculty of Pharmaceutical Sciences, Doshisha Women's College of Liberal Arts, Kyotanabe, Kyoto, 610-0395, Japan.<br /><searchLink fieldCode="AU" term="%22Kawasaki+K%22">Kawasaki K</searchLink>; Faculty of Pharmaceutical Sciences, Doshisha Women's College of Liberal Arts, Kyotanabe, Kyoto, 610-0395, Japan. Electronic address: kkawasak@dwc.doshisha.ac.jp. – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%220372516%22">Biochemical and biophysical research communications</searchLink> [Biochem Biophys Res Commun] 2026 Sep 03; Vol. 829, pp. 154186. <i>Date of Electronic Publication: </i>2026 Jun 22. – Name: TypePub Label: Publication Type Group: TypPub Data: Journal Article – Name: TitleSource Label: Journal Info Group: Src Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Elsevier%22">Elsevier </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>0372516 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1090-2104 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%220006291X%22">0006291X </searchLink><i>NLM ISO Abbreviation: </i>Biochem Biophys Res Commun <i>Subsets: </i>MEDLINE |
| PLink | https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=mdl&AN=42341419 |
| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.bbrc.2026.154186 Languages: – Code: eng Text: English PhysicalDescription: Pagination: StartPage: 154186 Titles: – TitleFull: The D-enantiomer of the antimicrobial peptide KLKLLLLLKLK-NH2 preferentially binds to lipopolysaccharide assemblies stabilized by divalent cations. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Sato S – PersonEntity: Name: NameFull: Kawasaki K IsPartOfRelationships: – BibEntity: Dates: – D: 03 M: 09 Text: 2026 Sep 03 Type: published Y: 2026 Identifiers: – Type: issn-electronic Value: 1090-2104 Numbering: – Type: volume Value: 829 Titles: – TitleFull: Biochemical and biophysical research communications Type: main |
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