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dc.contributor.advisor Diederichsen, Ulf Prof. Dr.
dc.contributor.author Höger, Geralin
dc.date.accessioned 2019-08-06T10:25:43Z
dc.date.available 2019-08-06T10:25:43Z
dc.date.issued 2019-08-06
dc.identifier.uri http://hdl.handle.net/21.11130/00-1735-0000-0003-C187-A
dc.language.iso eng de
dc.publisher Niedersächsische Staats- und Universitätsbibliothek Göttingen de
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.ddc 540 de
dc.title Self-Organization of β-Peptide Nucleic Acid Helices for Membrane Scaffolding de
dc.type doctoralThesis de
dc.contributor.referee Diederichsen, Ulf Prof. Dr.
dc.date.examination 2019-02-14
dc.description.abstracteng In a vast number of cellular processes interactions between membranes and proteins are essential, resulting in the lipid bilayer being interspersed immensely with proteins. Apart from catalytic or signaling functions, a tremendous amount of proteins is constituted of cytoskeletal components which line the cytoplasmic side of the plasma membrane as a mesh-like network and provide stability and shape of the cell. Numerous studies have been conducted to apprehend this so-called membrane skeleton and its underlying dynamics, however, many aspects remain obscure. Therefore, model systems with reduced complexity and specific interaction sites became a valuable tool to study the influence of peripheral networks on lipid bilayers. In this study, the design, synthesis and investigation of an artificial model system based on β-peptide nucleic acid (β-PNA) helices in order to assess the requirements for an aggregational system on lipid bilayer surfaces is displayed. After optimization of the solid phase peptide synthesis (SPPS) conditions to attain higher synthesis efficiency, different β-PNA systems with and without hydrophobic modifications for membrane attachment were realized and characterized by circular dichroism (CD) spectroscopy. Analyses conducted in solution via fluorescence spectroscopy and CD spectroscopy revealed the potential of β-PNA helices without hydrophobic modifications to form dimers which can be controlled by the number and sequence of the interacting nucleobases as well as by temperature. Furthermore, analyses conducted on membrane surfaces using β-PNA helices with hydrophobic modifications revealed simultaneous β-PNA/β-PNA and β-PNA/membrane interaction. de
dc.contributor.coReferee Steinem, Claudia Prof. Dr.
dc.subject.eng solid phase peptide synthesis (SPPS) de
dc.subject.eng membrane scaffolding de
dc.subject.eng membrane-associated protein networks de
dc.subject.eng β-peptide nucleic acids (β-PNA) de
dc.subject.eng circular dichroism (CD) spectroscopy de
dc.subject.eng fluorescence resonance energy transfer (FRET) de
dc.subject.eng fluorescence spectroscopy de
dc.subject.eng ultraviolet–visible (UV/Vis) spectroscopy de
dc.identifier.urn urn:nbn:de:gbv:7-21.11130/00-1735-0000-0003-C187-A-7
dc.affiliation.institute Fakultät für Chemie de
dc.subject.gokfull Chemie  (PPN62138352X) de
dc.identifier.ppn 1672307228

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