Carnarius, Christian

[["dc.bibliographiccitation.firstpage","879"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","MedChemComm"],["dc.bibliographiccitation.lastpage","886"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Ries, Oliver"],["dc.contributor.author","Carnarius, Christian"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Ducho, Christian"],["dc.date.accessioned","2015-07-17T07:56:31Z"],["dc.date.accessioned","2021-10-27T13:12:17Z"],["dc.date.available","2015-07-17T07:56:31Z"],["dc.date.available","2021-10-27T13:12:17Z"],["dc.date.issued","2015"],["dc.description.abstract","Functional insights into bioactive natural products with medicinal potential are often hindered by their structural complexity. We herein report a simplified model system to investigate the functional significance of a structural motif of biologically potent muraymycin antibiotics of the A-series. These compounds have a highly unusual ω-guanidinylated fatty acid moiety, which has been proposed to mediate membrane penetration, thus enabling the interaction of A-series muraymycins with their intracellular target MraY. Our assay was based on a synthetic conjugate of this fatty acid structure with a negatively charged fluorophore lacking membrane permeability. Using this conjugate, immobilised giant unilamellar lipid vesicles and confocal laser scanning fluorescence microscopy, we demonstrated that the attachment of the ω-N-hydroxyguanidinyl fatty acid unit led to an enhanced uptake of the fluorophore into the vesicles. This represents the first experimental evidence of this unusual structural motif's functional relevance for the parent natural product, which may support the future design of novel muraymycin analogues."],["dc.identifier.doi","10.1039/c4md00526k"],["dc.identifier.gro","3141982"],["dc.identifier.isi","000354437800016"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11974"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91677"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","2040-2511"],["dc.relation.issn","2040-2511"],["dc.relation.issn","2040-2503"],["dc.relation.orgunit","Fakultät für Chemie"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","fatty acid; moiety; muraymycin antibiotics; Membrane-interacting"],["dc.title","Membrane-interacting properties of the functionalised fatty acid moiety of muraymycin antibiotics"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4767"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Langmuir"],["dc.bibliographiccitation.lastpage","4774"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Neubacher, Henrik"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Carnarius, Christian"],["dc.contributor.author","Lazzara, Thomas D."],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:46:17Z"],["dc.date.available","2017-09-07T11:46:17Z"],["dc.date.issued","2014"],["dc.description.abstract","Screening tools to study antimicrobial peptides (AMPs) with the aim to optimize therapeutic delivery vectors require automated and parallelized sampling based on chip technology. Here, we present the development of a chip-based assay that allows for the investigation of the action of AMPs on planar lipid membranes in a time-resolved manner by fluorescence readout. Anodic aluminum oxide (AAO) composed of cylindrical pores with a diameter of 70 nm and a thickness of up to 10 mu m was used as a support to generate pore-spanning lipid bilayers from giant unilamellar vesicle spreading, which resulted in large continuous membrane patches sealing the pores. Because AAO is optically transparent, fluid single lipid bilayers and the underlying pore cavities can be readily observed by three-dimensional confocal laser scanning microscopy (CLSM). To assay the permeabilizing activity of the AMPs, the translocation of the water-soluble dyes into the AAO cavities and the fluorescence of the sulforhodamine 101 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanol-l-amine triethylammonium salt (Texas Red DHPE)-labeled lipid membrane were observed by CLSM in a time-resolved manner as a function of the AMP concentration. The effect of two different AMPs, magainin-2 and melittin, was investigated, showing that the concentrations required for membrane permeabilization and the kinetics of the dye entrance differ significantly. Our results are discussed in light of the proposed permeabilization models of the two AMPs. The presented data demonstrate the potential of this setup for the development of an on-chip screening platform for AMPs."],["dc.identifier.doi","10.1021/la500358h"],["dc.identifier.gro","3142140"],["dc.identifier.isi","000335297300029"],["dc.identifier.pmid","24707859"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4988"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft (DFG) [SFB 803]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0743-7463"],["dc.title","Permeabilization Assay for Antimicrobial Peptides Based on Pore-Spanning Lipid Membranes on Nanoporous Alumina"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6935"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","ACS Nano"],["dc.bibliographiccitation.lastpage","6944"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Lazzara, Thomas D."],["dc.contributor.author","Carnarius, Christian"],["dc.contributor.author","Kocun, Marta"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:43:25Z"],["dc.date.available","2017-09-07T11:43:25Z"],["dc.date.issued","2011"],["dc.description.abstract","Anodic aluminum oxide (AAO) is a porous material having aligned cylindrical compartments with 55-60 nm diameter pores, and being several micrometers deep. A protocol was developed to generate pore-spanning fluid lipid bilayers separating the attoliter-sized compartments of the nanoporous material from the bulk solution, while preserving the optical transparency of the AAO. The AAO was selectively functionalized by silane chemistry to spread giant unilamellar vesicles (GUVs) resulting In large continuous membrane patches covering the pores. Formation of fluid single lipid bilayers through GUV rupture could be readily observed by fluorescence microscopy and further supported by conservation of membrane surface area, before and after GUV rupture. Fluorescence recovery after photobleaching gale low immobile fractions (5-15%) and lipid diffusion coefficients similar to those found for bilayers on silica. The entrapment of molecules within the porous underlying cylindrical compartments, as well as the exclusion of macromolecules from the nanopores, demonstrate the barrier fun ton of the pore-spanning membranes and could be investigated in three-dimensions using confocal laser scanning fluorescence imaging."],["dc.identifier.doi","10.1021/nn201266e"],["dc.identifier.gro","3142672"],["dc.identifier.isi","000295187400021"],["dc.identifier.pmid","21797231"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/101"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1936-086X"],["dc.relation.issn","1936-0851"],["dc.title","Separating Attoliter-Sized Compartments Using Fluid Pore-Spanning Lipid Bilayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2877"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","2886"],["dc.bibliographiccitation.volume","287"],["dc.contributor.author","Carnarius, Christian"],["dc.contributor.author","Kreir, Mohamed"],["dc.contributor.author","Krick, Marcel"],["dc.contributor.author","Methfessel, Christoph"],["dc.contributor.author","Moehrle, Volker"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Brüggemann, Andrea"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Fertig, Niels"],["dc.date.accessioned","2017-09-07T11:49:01Z"],["dc.date.available","2017-09-07T11:49:01Z"],["dc.date.issued","2012"],["dc.description.abstract","In mammalian tissues, connexin 43 (Cx43) is the most prominent member of the connexin family. In a single lipid bilayer, six connexin subunits assemble into a hemichannel (connexon). Direct communication of apposing cells is realized by two adjacent hemichannels, which can form gap junction channels. Here, we established an expression system in Pichia pastoris to recombinantly produce and purify Cx43 as well as Cx43 fused to green fluorescent protein (GFP). Proteins were isolated from crude cell membrane fractions via affinity chromatography. Cx43 and Cx43-GFP hemichannels were reconstituted in giant unilamellar vesicles as proven by fluorescence microscopy, and their electrophysiological behavior was analyzed on the single channel level by planar patch clamping. Cx43 and Cx43-GFP both showed an ohmic behavior and a voltage-dependent open probability. Cx43 hemichannels exhibited one major mean conductance of 224 +/- 26 picosiemens (pS). In addition, a subconductance state at 124 +/- 5 pS was identified. In contrast, the analysis of Cx43-GFP single channels revealed 10 distinct conductance states in the range of 15 to 250 pS, with a larger open probability at 0 mV as compared with Cx43, which suggests that intermolecular interactions between the GFP molecules alter the electrophysiology of the protein."],["dc.identifier.doi","10.1074/jbc.M111.319871"],["dc.identifier.gro","3142586"],["dc.identifier.isi","000300292300059"],["dc.identifier.pmid","22139870"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8953"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9258"],["dc.title","Green Fluorescent Protein Changes the Conductance of Connexin 43 (Cx43) Hemichannels Reconstituted in Planar Lipid Bilayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]