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Selective Antibacterial Activity and Lipid Membrane Interactions of Arginine-Rich Amphiphilic Peptides

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dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en
dc.contributor.author Edwards-Gayle, Charlotte J.C.
dc.contributor.author Barrett, Glyn
dc.contributor.author Roy, Shyamali
dc.contributor.author Castelletto, Valeria
dc.contributor.author Seitsonen, Jani
dc.contributor.author Ruokolainen, Janne
dc.contributor.author Hamley, Ian W.
dc.date.accessioned 2020-11-30T08:20:55Z
dc.date.available 2020-11-30T08:20:55Z
dc.date.issued 2020-02-17
dc.identifier.citation Edwards-Gayle , C J C , Barrett , G , Roy , S , Castelletto , V , Seitsonen , J , Ruokolainen , J & Hamley , I W 2020 , ' Selective Antibacterial Activity and Lipid Membrane Interactions of Arginine-Rich Amphiphilic Peptides ' , ACS Applied Bio Materials , vol. 3 , no. 2 , pp. 1165-1175 . https://doi.org/10.1021/acsabm.9b00894 en
dc.identifier.issn 2576-6422
dc.identifier.other PURE UUID: edd633c4-9244-45b5-b82c-b4bf55724c09
dc.identifier.other PURE ITEMURL: https://research.aalto.fi/en/publications/selective-antibacterial-activity-and-lipid-membrane-interactions-of-argininerich-amphiphilic-peptides(edd633c4-9244-45b5-b82c-b4bf55724c09).html
dc.identifier.other PURE LINK: http://www.scopus.com/inward/record.url?scp=85080086363&partnerID=8YFLogxK
dc.identifier.other PURE FILEURL: https://research.aalto.fi/files/53503846/Selective_Antibacterial_Activity.acsabm.9b00894.pdf
dc.identifier.uri https://aaltodoc.aalto.fi/handle/123456789/61830
dc.description.abstract The self-assembly behavior and antimicrobial activity of two designed amphiphilic peptides, R3F3 and R4F4, containing short hydrophobic phenylalanine (F) and cationic arginine (R) sequences, are investigated. The conformation of the peptides was examined using circular dichroism and FTIR spectroscopy, which show that they have a disordered secondary structure. Concentration-dependent fluorescence assays show the presence of a critical aggregation concentration (cac) for each peptide. Above the cac, small-angle X-ray scattering (SAXS) and transmission electron microscopy (TEM) reveal a population of twisted tapes for R3F3 and nanosheets for R4F4. The interaction of the peptides with model bacterial membranes comprising mixtures of the lipids DPPG [1,2-dipalmitoyl-sn-glycero-3-phosphoglycerol] and DPPE [1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine], was studied using SAXS and cryogenic-TEM. Analysis of the SAXS structure factor indicates that R3F3 interacts with lipid bilayers by inducing correlation between bilayers, whereas R4F4 interacts with the bilayers causing an increase in polydispersity of the vesicle wall thickness. Both peptides break vesicles with a 1:3 DPPG:DPPE composition, which is close to the ratio of PG and PE lipids observed in the lipid membrane of Pseudomonas aeruginosa, a pathogen responsible for serious infections and which has developed antimicrobial resistant strains. Both peptides show activity against this bacterium in planktonic form. Peptide R4F4 shows particularly strong bioactivity against this microbe, with a minimum inhibitory concentration (MIC) value in the range of concentrations where the peptide is cytocompatible. It was further shown to have activity against other Pseudomonas species including the common plant pathogen Pseudomonas syringae. Finally, we show that R4F4 inhibits the development of P. aeruginosa biofilms. This was examined in detail and a proposed mechanism involving binding of the signaling molecule c-di-GMP is suggested, based on circular dichroism spectroscopy studies and Congo red assays of extracellular polysaccharides produced by the stressed bacteria. Thus, R4F4 is a promising candidate antimicrobial peptide with activity against Pseudomonas species. en
dc.format.extent 11
dc.format.extent 1165-1175
dc.format.mimetype application/pdf
dc.language.iso en en
dc.relation.ispartofseries ACS Applied Bio Materials en
dc.relation.ispartofseries Volume 3, issue 2 en
dc.rights openAccess en
dc.title Selective Antibacterial Activity and Lipid Membrane Interactions of Arginine-Rich Amphiphilic Peptides en
dc.type A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä fi
dc.description.version Peer reviewed en
dc.contributor.department University of Reading
dc.contributor.department Department of Applied Physics
dc.contributor.department Molecular Materials
dc.subject.keyword antimicrobial
dc.subject.keyword liposomes
dc.subject.keyword model membranes
dc.subject.keyword peptide
dc.subject.keyword SAXS
dc.subject.keyword self-assembly
dc.identifier.urn URN:NBN:fi:aalto-2020113020675
dc.identifier.doi 10.1021/acsabm.9b00894
dc.type.version publishedVersion

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