Diederichsen, Ulf

[["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","2336"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","ChemPhysChem"],["dc.bibliographiccitation.lastpage","2343"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Kuesel, Andrea"],["dc.contributor.author","Khattari, Ziad"],["dc.contributor.author","Schneggenburger, Philipp Erik"],["dc.contributor.author","Banerjee, Arnab"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2017-09-07T11:49:23Z"],["dc.date.available","2017-09-07T11:49:23Z"],["dc.date.issued","2007"],["dc.description.abstract","Peptides with alternating amino acid configuration provide helical secondary structures that are especially known from the membrane channel and pore-forming gramicidin A. In analogy to this natural D,L-alternating pentadecapeptide, the potential of D,L-alternating peptides for membrane insertion is investigated using the model dodecamer peptide H-(Phe-Tyr)(5)-Trp-Trp-OH. This aromatic peptide is introduced as a novel pore-forming synthetic analogue of gramicidin A. It forms a well-organized homodimer similar to one of the gromicidin A transmembrane motifs."],["dc.identifier.doi","10.1002/cphc.200700477"],["dc.identifier.gro","3143411"],["dc.identifier.isi","000251004200007"],["dc.identifier.pmid","17935092"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/922"],["dc.notes.intern","WoS Import 2017-03-10"],["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","membrane biophysics"],["dc.title","Conformation and interaction of a D,L-alternating peptide with a bilayer membrane: X-ray reflectivity, CD, and FTIR spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]