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Citation link: http://nbn-resolving.de/urn:nbn:de:gbv:46-00106931-10
00106931-1.pdf
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Binding affinities and adhesion phenomena of binding peptides at the interface to zinc oxide


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00106931-1.pdf131.93 MBAdobe PDFView/Open
Other Titles: Bindungsaffinitäten und -phänomene an der Grenzfläche zwischen Peptiden und Zinkoxid
Authors: Michaelis, Monika  
Supervisor: Colombi Ciacchi, Lucio
1. Expert: Colombi Ciacchi, Lucio
2. Expert: Epple, Matthias 
Abstract: 
Peptide sequences can selectively bind to inorganic substrates in a process similar to the concept of molecular recognition. Here we focused on zinc oxide as an important representative of functional oxides and identified binding peptides with an affinity for different ZnO facets. Five peptides were selected and their conformational ensemble (macrostate) and sensitivity to adsorption were characterised via circular dichroism (CD) spectroscopy. The microstates within their conformational ensembles are accessed by enhanced sampling simulations. To quantify the free energies of adsorption, an optically sectioned indicator displacement assay (O-IDA) was adapted to the peptide/ZnO interface and compared to the results of single molecule force spectroscopy (SMFS), leading to a good agreement between the two approaches.
Keywords: zinc oxide, binding peptides, circular dichroism spectroscopy, single molecule force spectroscopy, indicator displacement assay
Issue Date: 20-Nov-2018
Type: Dissertation
URN: urn:nbn:de:gbv:46-00106931-10
Institution: Universität Bremen 
Faculty: FB4 Produktionstechnik 
Appears in Collections:Dissertationen

  

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