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Zitierlink URN
https://nbn-resolving.de/urn:nbn:de:gbv:46-00102824-14

Peptidbasierte Materialentwicklung

Veröffentlichungsdatum
2012-07-26
Autoren
Richter, Katharina  
Betreuer
Hartwig, Andreas  
Gutachter
Montforts, Franz-Peter  
Zusammenfassung
Adhesion represents a key joining technology and nature has been developing adhesives for millions of years. These biological adhesives can be found in all natural habitats, where they perform extraordinary bonding, partly under extreme conditions. For example, the blue marine mussel Mytilus edulis is able to adhere to a number of surfaces in sea water: e.g. glass, plastic, metal, wood, and even PTFE. The transfer of these bonding properties to technical and medical adhesives represents a major challenge, but also could lead to enormous benefits for industrial technology or medical treatment. Although the composition of protein based adhesives, as the ones of marine mussel are well known currently, the exact principles of the initial interactions with surfaces remains unclear. For the development of new bioinspired adhesives a potential way is the assessment of the adsorption properties of some mussel inspired peptides towards titanium and silica. For evaluating the influence of the essential amino acid DOPA, derivatives of the mussel peptide Mefp-1 were synthesised by solid phase peptide synthesis. The effect of sequence length and oxidation state was investigated using the quartz crystal microbalance (QCM) technique. This method was supplemented with XPS-analytics. Additionally, the tensile strengths of peptide glued tooth fragments were determined. Furthermore the eligibility of the peptide to perform e.g. with adhesional properties, after it was bioconjugated or immobilised on a surface, were investigated.
Schlagwörter
peptide, surface, adhesion, immobilisation, DOPA
Institution
Universität Bremen  
Fachbereich
Fachbereich 02: Biologie/Chemie (FB 02)  
Dokumenttyp
Dissertation
Zweitveröffentlichung
Nein
Sprache
Deutsch
Dateien
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Vorschaubild
Name

00102824-1.pdf

Size

6.44 MB

Format

Adobe PDF

Checksum

(MD5):b433bd160e3d272f155b324b386d913f

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