Worbs, Brigitte

[["dc.bibliographiccitation.firstpage","1567"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","ChemPhysChem"],["dc.bibliographiccitation.lastpage","1576"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Schneggenburger, Philipp Erik"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Worbs, Brigitte"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2017-09-07T11:46:52Z"],["dc.date.available","2017-09-07T11:46:52Z"],["dc.date.issued","2009"],["dc.description.abstract","Structural parameters, such as conformation, orientation and penetration depth of membrane-bound peptides and proteins that may function as channels, pores or biocatalysts, are of persistent interest and have to be probed in the native fluid state of a membrane. X-ray scattering in combination with heavy-atom labeling is a powerful and highly appropriate method to reveal the position of a certain amino acid residue within a lipid bilayer with respect to the membrane normal axis up to a resolution of several Angstrom. Herein, we report the synthesis of a new iodine-labeled amino acid building block. This building block is intended for peptide incorporation to provide high intensities for electron density difference analysis of X-ray reflectivity data and improve the labeling potential for the lipid bilayer head-group and water region. The novel building block as well as the commercially available non-iodinated analogue, required for X-ray scattering, was implemented in a transmembrane peptide motif via manual solid-phase peptide synthesis (SPPS) following the fluorenylmethyloxycarbonyl (Fmoc)-strategy. The derived peptides were reconstituted in lipid vesicles as well as in highly aligned multilamellar lipid stacks and investigated via circular dichroism (CD) and X-ray reflectivity. Thereby, it has been revealed that the bulky iodine probe neither causes conformational change of the peptide structure nor lamellar disordering of the membrane complexes."],["dc.identifier.doi","10.1002/cphc.200900241"],["dc.identifier.gro","3143086"],["dc.identifier.isi","000267928100032"],["dc.identifier.pmid","19565579"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/561"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [SFB 803]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1439-4235"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","A Novel Heavy-Atom Label for Side-Specific Peptide Iodination: Synthesis, Membrane Incorporation and X-ray Reflectivity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8020"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","8028"],["dc.bibliographiccitation.volume","132"],["dc.contributor.author","Schneggenburger, Philipp Erik"],["dc.contributor.author","Müllar, Stefan"],["dc.contributor.author","Worbs, Brigitte"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2017-09-07T11:46:00Z"],["dc.date.available","2017-09-07T11:46:00Z"],["dc.date.issued","2010"],["dc.description.abstract","The aggregation and organization of membrane proteins and transmembrane peptides is related to the interacting molecular species itself and strongly depends on the lipid environment. Because of the complexity and dynamics of these interactions, they are often hardly traceable and nearly impossible to predict. For this reason, peptide model systems are a valuable tool in studying membrane associated processes since they are synthetically accessible and can be readily modified. To control and study the aggregation of peptide transmembrane domains (TMDs) the interacting interfaces of the TMDs themselves can be altered. A second less extensively studied approach targets the TMD assembly by using interaction and recognition of domains at the membrane outside as frequently found in the membrane protein interplay and protein assembly. In the present study, double helical transmembrane domains were designed and synthesized on the basis of a recently reported D,L-alternating peptide pore motif derived from gramicidin A. The highly hydrophobic and aromatic transmembrane peptide was covalently functionalized with a short peptide nucleic acid (PNA) used as specific outer-membrane recognition unit. The PNA sequences were chosen with high polarity to ensure localization within the aqueous phase. To estimate the impact of the membrane adjacent recognition on the TMD assembly by Forster resonance energy transfer (FRET), fluorescence probes were covalently attached to the side chains of the membrane spanning peptide helices. Dimerization of the TMD-peptide/PNA conjugates within unilamellar lipid vesicles was observed. The dimer/monomer ratio of TMDs can be controlled by temperature variation."],["dc.identifier.doi","10.1021/ja1006349"],["dc.identifier.gro","3142904"],["dc.identifier.isi","000278717700049"],["dc.identifier.pmid","20481532"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/360"],["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","0002-7863"],["dc.title","Molecular Recognition at the Membrane-Water Interface: Controlling Integral Peptide Helices by Off-Membrane Nucleobase Pairing"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Peptide Science"],["dc.bibliographiccitation.lastpage","14"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Schneggenburger, Philipp E."],["dc.contributor.author","Worbs, Brigitte"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2018-11-07T08:48:03Z"],["dc.date.available","2018-11-07T08:48:03Z"],["dc.date.issued","2010"],["dc.description.abstract","Peptide azides acquired growing impact because of application in bioconjugation via 'click chemistry' or Staudinger ligation. Furthermore, there are many methods established in organic synthesis addressing the reduction of azides to amines, but no observation of a reductive transformation of peptide azides during SPPS cleavage was yet reported. In the present study, the reduction of peptide azides during SPPS cleavage was investigated depending on the choice of thioscavenger, reacting as reductive species. First observed for short PNA/peptide conjugates the occurring extensive side reaction was also validated for one of the applied azide amino acid building blocks and was further investigated by applying different cleavage cocktails to a series of peptides varying in hydrophobicity and position of the azide moiety in the oligomer sequence. Copyright (C) 2009 European Peptide Society and John Wiley & Sons, Ltd."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB 803]"],["dc.identifier.doi","10.1002/psc.1202"],["dc.identifier.isi","000273453400003"],["dc.identifier.pmid","19950105"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21109"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","John Wiley & Sons Ltd"],["dc.relation.issn","1075-2617"],["dc.title","Azide reduction during peptide cleavage from solid support - the choice of thioscavenger?"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]