Sibold, Jeremias

[["dc.bibliographiccitation.firstpage","14175"],["dc.bibliographiccitation.issue","49"],["dc.bibliographiccitation.journal","Langmuir : the ACS journal of surfaces and colloids"],["dc.bibliographiccitation.lastpage","14183"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Teske, Nelli"],["dc.contributor.author","Sibold, Jeremias"],["dc.contributor.author","Schumacher, Johannes"],["dc.contributor.author","Teiwes, Nikolas K."],["dc.contributor.author","Gleisner, Martin"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2018-01-17T13:00:51Z"],["dc.date.available","2018-01-17T13:00:51Z"],["dc.date.issued","2017"],["dc.description.abstract","A number of techniques has been developed and analyzed in recent years to generate pore-spanning membranes (PSMs). While quite a number of methods rely on nanoporous substrates, only a few use micrometer-sized pores to be able to individually resolve suspending membranes by means of fluorescence microscopy. To be able to produce PSMs on pores that are micrometer in size, an orthogonal functionalization strategy resulting in a hydrophilic surface is highly desirable. Here, we report on a method to prepare PSMs based on the evaporation of a thin layer of silicon monoxide on top of the porous substrate. PM-IRRAS experiments demonstrate that the final surface is composed of SiOx with 1 < x < 2. The hydrophilic surface turned out to be well suited to spread giant unilamellar vesicles forming PSMs. As the method does not rely on a gold coating as frequently used for orthogonal functionalization, fluorescence micrographs provide information not only from the freestanding membrane areas but also from the supported ones. The observation of the entire PSM area enabled us to observe phase-separation in these membranes on the freestanding and supported parts as well as protein binding and possible lipid reorganization of the membranes induced by binding of the protein Shiga toxin."],["dc.identifier.doi","10.1021/acs.langmuir.7b02727"],["dc.identifier.pmid","29148811"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11698"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1520-5827"],["dc.title","Continuous Pore-Spanning Lipid Bilayers on Silicon Oxide-Coated Porous Substrates"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","15630"],["dc.bibliographiccitation.issue","28"],["dc.bibliographiccitation.journal","Physical Chemistry, Chemical Physics"],["dc.bibliographiccitation.lastpage","15638"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Bosse, Mathias"],["dc.contributor.author","Sibold, Jeremias"],["dc.contributor.author","Scheidt, Holger A."],["dc.contributor.author","Patalag, Lukas J."],["dc.contributor.author","Kettelhoit, Katharina"],["dc.contributor.author","Ries, Annika"],["dc.contributor.author","Werz, Daniel B."],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Huster, Daniel"],["dc.date.accessioned","2020-12-10T18:11:27Z"],["dc.date.available","2020-12-10T18:11:27Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1039/C9CP02501D"],["dc.identifier.eissn","1463-9084"],["dc.identifier.issn","1463-9076"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16738"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74015"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0"],["dc.title","Shiga toxin binding alters lipid packing and the domain structure of Gb 3 -containing membranes: a solid-state NMR study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2171"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","Chembiochem : a European journal of chemical biology"],["dc.bibliographiccitation.lastpage","2178"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Patalag, Lukas J."],["dc.contributor.author","Sibold, Jeremias"],["dc.contributor.author","Schütte, Ole M."],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Werz, Daniel B."],["dc.date.accessioned","2018-01-17T13:01:43Z"],["dc.date.available","2018-01-17T13:01:43Z"],["dc.date.issued","2017"],["dc.description.abstract","Glycosphingolipids are involved in a number of physiological and pathophysiological processes, and they serve as receptors for a variety of bacterial toxins and viruses. To investigate their function in lipid membranes, fluorescently labeled glycosphingolipids are highly desirable. Herein, a synthetic route to access Gb3 glycosphingolipids with fluorescently labeled fatty acids, consisting of pentaene and hexaene moieties either at the terminus or in the middle of the acyl chain, has been developed. The fluorescent properties of the Gb3 derivatives were investigated in small unilamellar vesicles composed of a raft-like mixture. Phase-separated giant unilamellar vesicles (GUVs) allowed the quantification of the apparent partitioning coefficients of the Gb3 compounds by means of confocal fluorescence laser scanning microscopy. The determined partition coefficients demonstrate that the Gb3 derivatives are preferentially localized in the liquid-disordered (ld ) phase. To analyze whether the compounds behave like their physiological counterparts, Cy3-labeled (Cy: cyanine) Shiga toxin B subunits (STxB) were specifically bound to Gb3 -doped GUVs. However, the protein was favorably localized in the ld phase, in contrast to results reported for STxB bound to naturally occurring Gb3 , which is discussed in terms of the packing density of the lipids in the liquid-ordered (lo ) phase."],["dc.identifier.doi","10.1002/cbic.201700414"],["dc.identifier.pmid","28941080"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11699"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1439-7633"],["dc.title","Gb3 Glycosphingolipids with Fluorescent Oligoene Fatty Acids: Synthesis and Phase Behavior in Model Membranes"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2670"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","The Analyst"],["dc.bibliographiccitation.lastpage","2677"],["dc.bibliographiccitation.volume","142"],["dc.contributor.author","Schwamborn, Miriam"],["dc.contributor.author","Schumacher, Johannes"],["dc.contributor.author","Sibold, Jeremias"],["dc.contributor.author","Teiwes, Nikolas K."],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2018-01-17T13:03:01Z"],["dc.date.available","2018-01-17T13:03:01Z"],["dc.date.issued","2017"],["dc.description.abstract","Monitoring the proton pumping activity of proteins such as ATPases in reconstituted single proteoliposomes is key to quantify the function of proteins as well as potential proton pump inhibitors. However, most pH-detecting assays available are either not quantitative, require well-adapted reconstitution protocols or are not appropriate for single vesicle studies. Here, we describe the quantitative and time-resolved detection of F-type ATPase-induced pH changes across vesicular membranes doped with the commercially available pH sensitive fluorophore Oregon Green 488 DHPE. This dye is shown to be well suited to monitor acidification of lipid vesicles not only in bulk but also at the single vesicle level. The pKa value of Oregon Green 488 DHPE embedded in a lipid environment was determined to be 6.1 making the fluorophore well suited for a variety of physiologically relevant proton pumps. The TFOF1-ATPase from a thermophilic bacterium was reconstituted into large unilamellar vesicles and the bulk acidification assay clearly reveals the overall activity of the F-type ATPase in the vesicle ensemble with an average pH change of 0.45. However, monitoring the pH changes in individual vesicles attached to a substrate demonstrates that the fraction of vesicles with a significant observable pH change is only about 5%, a number that cannot be gathered from bulk experiments and which is considerably lower than expected."],["dc.identifier.doi","10.1039/c7an00215g"],["dc.identifier.pmid","28616949"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11701"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1364-5528"],["dc.title","Monitoring ATPase induced pH changes in single proteoliposomes with the lipid-coupled fluorophore Oregon Green 488"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","17805"],["dc.bibliographiccitation.issue","49"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","17813"],["dc.bibliographiccitation.volume","58"],["dc.contributor.author","Sibold, Jeremias"],["dc.contributor.author","Kettelhoit, Katharina"],["dc.contributor.author","Vuong, Loan"],["dc.contributor.author","Liu, Fangyuan"],["dc.contributor.author","Werz, Daniel B."],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2019-11-13T15:23:59Z"],["dc.date.accessioned","2021-10-27T13:12:45Z"],["dc.date.available","2019-11-13T15:23:59Z"],["dc.date.available","2021-10-27T13:12:45Z"],["dc.date.issued","2019"],["dc.description.abstract","The receptor lipid Gb3 is responsible for the specific internalization of Shiga toxin (STx) into cells. The head group of Gb3 defines the specificity of STx binding, and the backbone with different fatty acids is expected to influence its localization within membranes impacting membrane organization and protein internalization. To investigate this influence, a set of Gb3 glycosphingolipids labeled with a BODIPY fluorophore attached to the head group was synthesized. C24 fatty acids, saturated, unsaturated, α-hydroxylated derivatives, and a combination thereof, were attached to the sphingosine backbone. The synthetic Gb3 glycosphingolipids were reconstituted into coexisting liquid-ordered (lo )/liquid-disordered (ld ) giant unilamellar vesicles (GUVs), and STx binding was verified by fluorescence microscopy. Gb3 with the C24:0 fatty acid partitioned mostly in the lo phase, while the unsaturated C24:1 fatty acid distributes more into the ld phase. The α-hydroxylation does not influence its partitioning."],["dc.identifier.doi","10.1002/anie.201910148"],["dc.identifier.eissn","1521-3773"],["dc.identifier.issn","1433-7851"],["dc.identifier.pmid","31529754"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16659"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91719"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.issn","1433-7851"],["dc.relation.orgunit","Fakultät für Chemie"],["dc.rights","CC BY 4.0"],["dc.rights.access","openAccess"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject","carbohydrates; fatty acids; fluorescence; membranes; toxins"],["dc.subject.ddc","540"],["dc.title","Synthesis of Gb3 Glycosphingolipids with Labeled Head Groups: Distribution in Phase-Separated Giant Unilamellar Vesicles"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9308"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","Physical Chemistry Chemical Physics"],["dc.bibliographiccitation.lastpage","9315"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Sibold, Jeremias"],["dc.contributor.author","Tewaag, Vera E."],["dc.contributor.author","Vagedes, Thomas"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2021-04-14T08:26:44Z"],["dc.date.available","2021-04-14T08:26:44Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1039/d0cp00335b"],["dc.identifier.eissn","1463-9084"],["dc.identifier.issn","1463-9076"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82058"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1463-9084"],["dc.relation.issn","1463-9076"],["dc.title","Phase separation in pore-spanning membranes induced by differences in surface adhesion"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.contributor.author","Sibold, Jeremias"],["dc.contributor.author","Ahadi, Somayeh"],["dc.contributor.author","Werz, Daniel B."],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2021-04-14T08:23:37Z"],["dc.date.available","2021-04-14T08:23:37Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1007/s00249-020-01461-w"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80987"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.title","Chemically synthesized Gb3 glycosphingolipids: tools to access their function in lipid membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]