Self-Organization of β-Peptide Nucleic Acid Helices for Membrane Scaffolding

Höger, Geralin

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.identifier.uri	http://dx.doi.org/10.53846/goediss-7585
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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Fakultät für Chemie (inkl. GAUSS) [701]

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