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dc.contributor.authorAlliband, Amanda M.
dc.contributor.authorWang, Zifan
dc.contributor.authorThacker, Christopher
dc.contributor.authorEnglish, Douglas S.
dc.contributor.authorBurns, Dennis H.
dc.date.accessioned2015-01-13T03:17:44Z
dc.date.available2015-01-13T03:17:44Z
dc.date.issued2015
dc.identifier.citationAlliband, Amanda M.; Wang, Zifan; Thacker, Christopher; English, Douglas S.; Burns, Dennis H. 2015. Developing a targeting system for bacterial membranes: measuring receptor-phosphatidylglycerol interactions with H-1 NMR, ITC and fluorescence correlation spectroscopy. Organic & Biomolecular Chemistry, vol. 13:no. 2:pp 502-512en_US
dc.identifier.issn1477-0520
dc.identifier.otherWOS:000346048600022
dc.identifier.urihttp://dx.doi.org/10.1039/c4ob01895h
dc.identifier.urihttp://hdl.handle.net/10057/11040
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractAn ammonium picket porphyrin that targets bacterial membranes has been prepared and shown to bind to phosphatidylglycerol (PG), a bacterial lipid, when the lipid was in solution, contained within synthetic membrane vesicles, or when in Gram-negative and Gram-positive bacterial membranes. The multifunctional receptor was designed to interact with both the phosphate anion portion and neutral glycerol portion of the lipid headgroup. The receptor's affinity and selectivity for binding to surfactant vesicles or lipid vesicles that contain PG within their membranes was directly measured using fluorescence correlation spectroscopy (FCS). FCS demonstrated that the picket porphyrin's binding pocket was complementary for the lipid headgroup, since simple Coulombic interactions alone did not induce binding. H-1 NMR and isothermal titration calorimetry (ITC) were used to determine the receptor's binding stoichiometry, receptor-lipid complex structure, binding constant, and associated thermodynamic properties of complexation in solution. The lipid-receptor binding motif in solution was shown to mirror the binding motif of membrane-bound PG and receptor. Cell lysis assays with E. coli (Gram-negative) and Bacillus thuringiensis (Gram-positive) probed with UV/Visible spectrophotometry indicated that the receptor was able to penetrate either bacterial cell wall and to bind to the bacterial inner membrane.en_US
dc.language.isoen_USen_US
dc.publisherRoyal Society of Chemistryen_US
dc.relation.ispartofseriesOrganic & Biomolecular Chemistry;v.13:no.2
dc.subjectAntimicrobial peptidesen_US
dc.subjectBinding; stoichiometryen_US
dc.subjectSelectivityen_US
dc.subjectCerageninsen_US
dc.subjectPorphyrinsen_US
dc.subjectVesiclesen_US
dc.subjectDesignen_US
dc.titleDeveloping a targeting system for bacterial membranes: measuring receptor-phosphatidylglycerol interactions with H-1 NMR, ITC and fluorescence correlation spectroscopyen_US
dc.typeArticleen_US
dc.rights.holder© Royal Society of Chemistry 2015


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