Format:
XIV, 125
,
Illustrationen, Diagramme
Content:
The enzyme Sortase A catalyzes the formation of a peptide bond between the recognition sequence LPXTG and an oligoglycine. While manifold ligations between proteins and various biomolecules, proteins and small synthetic molecules as well as proteins and surfaces have been reported, the aim of this thesis was to investigate the sortase-catalyzed linkage between artificial building blocks. Hence, this could pave the way for the use of sortase A for tasks from a chemical point of view and maybe even materials science. For the proof of concept, the studied systems were kept as simple as possible at first by choosing easily accessible silica NPs and commercially available polymers. These building blocks were functionalized with peptide motifs for sortase-mediated ligation. Silica nanoparticles were synthesized with diameters of 60 and 200 nm and surface modified with C=C functionalities. Then, peptides bearing a terminal cysteine were covalently linked by means of a thiol-ene reaction. ...
Note:
Dissertation Universität Potsdam 2018
Additional Edition:
Erscheint auch als Online-Ausgabe Dai, Xiaolin Synthesis of artificial building blocks for sortase-mediated ligation and their enzymatic linkage Potsdam, 2018
Language:
English
Keywords:
Aminoacyltransferasen
;
Ligation
;
Siliciumdioxid
;
Peptid-Bindung
;
Hochschulschrift
Author information:
Böker, Alexander 1973-