Rost, Ulrike

[["dc.bibliographiccitation.journal","Chem. Sci."],["dc.contributor.author","Rost, U."],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Diederichsen, U."],["dc.date.accessioned","2016-06-09T11:12:42Z"],["dc.date.accessioned","2021-10-27T13:12:22Z"],["dc.date.available","2016-06-09T11:12:42Z"],["dc.date.available","2021-10-27T13:12:22Z"],["dc.date.issued","2016"],["dc.description.abstract","Transmembrane b-peptide helices and their association in lipid membranes are still widely unexplored. We designed and synthesized transmembrane b-peptides harboring different numbers of D-b3-glutamine residues (hGln) by solid phase peptide synthesis. By means of circular dichroism spectroscopic measurements, the secondary structure of the b-peptides reconstituted into unilamellar vesicles was determined to be similar to a right-handed 314-helix. Fluorescence spectroscopy using D-b3-tryptophan residues strongly suggested a transmembrane orientation. Two or three hGln served as recognition units between the helices to allow helix–helix assembly driven by hydrogen bond formation. The association state of the transmembrane b-peptides as a function of the number of hGln residues was investigated by fluorescence resonance energy transfer (FRET). Therefore, two fluorescence probes (NBD, TAMRA) were covalently attached to the side chains of the transmembrane b-peptide helices. The results clearly demonstrate that only b-peptides with hGln as recognition units assemble into oligomers, presumably trimers. Temperature dependent FRET experiments further show that the strength of the helix–helix association is a function of the number of hGln residues in the helix."],["dc.identifier.doi","10.1039/C6SC01147K"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13340"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91685"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.issn","2041-6539"],["dc.relation.issn","2041-6520"],["dc.relation.orgunit","Fakultät für Chemie"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","b-peptides;"],["dc.title","β-Glutamine-mediated self-association of transmembrane β-peptides within lipid bilayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2525"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","ChemPhysChem"],["dc.bibliographiccitation.lastpage","2534"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Rost, Ulrike"],["dc.contributor.author","Xu, Yihui"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2017-11-28T09:52:28Z"],["dc.date.available","2017-11-28T09:52:28Z"],["dc.date.issued","2016"],["dc.description.abstract","Transmembrane β-peptides are promising candidates for the design of well-controlled membrane anchors in lipid membranes. Here, we present the synthesis of transmembrane β-peptides with and without tryptophan anchors, as well as a novel iodine-labeled d-β3-amino acid. By using one or more of the heavy-atom labeled amino acids as markers, the orientation of the helical peptide was inferred based on the electron-density profile determined by X-ray reflectivity. The β-peptides were synthesized through manual Fmoc-based solid-phase peptide synthesis (SPPS) and reconstituted in unilamellar vesicles forming a right-handed 314-helix secondary structure, as shown by circular dichroism spectroscopy. We then integrated the β-peptide into solid-supported membrane stacks and carried out X-ray reflectivity and grazing incidence small-angle X-ray scattering to determine the β-peptide orientation and its effect on the membrane bilayers. These β-peptides adopt a well-ordered transmembrane motif in the solid-supported model membrane, maintaining the basic structure of the original bilayer with some distinct alterations. Notably, the helical tilt angle, which accommodates the positive hydrophobic mismatch, induces a tilt of the acyl chains. The tilted chains, in turn, lead to a membrane thinning effect."],["dc.identifier.doi","10.1002/cphc.201600289"],["dc.identifier.fs","622329"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/10566"],["dc.language.iso","en"],["dc.notes.status","public"],["dc.relation.issn","1439-4235"],["dc.title","Heavy-Atom Labeled Transmembrane β-Peptides: Synthesis, CD-Spectroscopy, and X-ray Diffraction Studies in Model Lipid Multilayer"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5900"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Chemical Science"],["dc.bibliographiccitation.lastpage","5907"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Rost, Ulrike"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2017-09-07T11:54:43Z"],["dc.date.available","2017-09-07T11:54:43Z"],["dc.date.issued","2016"],["dc.description.abstract","Transmembrane beta-peptide helices and their association in lipid membranes are still widely unexplored. We designed and synthesized transmembrane beta-peptides harboring different numbers of D-beta(3)-glutamine residues ((h)Gln) by solid phase peptide synthesis. By means of circular dichroism spectroscopic measurements, the secondary structure of the beta-peptides reconstituted into unilamellar vesicles was determined to be similar to a right-handed 3(14)-helix. Fluorescence spectroscopy using D-beta(3)-tryptophan residues strongly suggested a transmembrane orientation. Two or three (h)Gln served as recognition units between the helices to allow helix-helix assembly driven by hydrogen bond formation. The association state of the transmembrane b-peptides as a function of the number of (h)Gln residues was investigated by fluorescence resonance energy transfer (FRET). Therefore, two fluorescence probes (NBD, TAMRA) were covalently attached to the side chains of the transmembrane beta-peptide helices. The results clearly demonstrate that only beta-peptides with (h)Gln as recognition units assemble into oligomers, presumably trimers. Temperature dependent FRET experiments further show that the strength of the helix-helix association is a function of the number of hGln residues in the helix."],["dc.identifier.doi","10.1039/c6sc01147k"],["dc.identifier.gro","3141748"],["dc.identifier.isi","000382488500038"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/635"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [A01, SFB 803]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","2041-6539"],["dc.relation.issn","2041-6520"],["dc.title","β-Glutamine-mediated self-association of transmembrane beta-peptides within lipid bilayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]