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Self-Assembly of Spider Silk-Fusion Proteins Comprising Enzymatic and Fluorescence Activity

Title data

Humenik, Martin ; Mohrand, Madeleine ; Scheibel, Thomas:
Self-Assembly of Spider Silk-Fusion Proteins Comprising Enzymatic and Fluorescence Activity.
In: Bioconjugate Chemistry. (2018) . - 7 S..
ISSN 1520-4812
DOI: https://doi.org/10.1021/acs.bioconjchem.7b00759

Abstract in another language

The recombinant spider silk protein eADF4(C16) was genetically fused either with esterase 2 (EST2) or green fluorescent protein (GFP). The fusions EST-eADF4(C16) and GFP-eADF4(C16) were spectroscopically investigated and showed native structures of EST and GFP. The structural integrity was confirmed by the enzymatic activity of EST and the fluorescence of GFP. The spider silk moiety retained its intrinsically unstructured conformation in solution and the self-assembly into either nanofibrils or nanoparticles could be controlled by the concentration of phosphate. Particles, however, showed significantly lower activity of the EST and GFP domains likely caused by a steric hindrance. However, upon self-assembly of EST-eADF4-(C16) and GFP-eADF4(C16) into fibrils the protein activities were retained. In general, the fusion of globular enzymes with the spider silk domain allows the generation of fibrous biomaterials with catalytic or light emitting properties.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Spider Silk Protein; Fusion; EST; GFP; steric hindrance; catalytic
Institutions of the University: Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Chair Biomaterials
Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Emerging Fields
Profile Fields > Emerging Fields > Food and Health Sciences
Research Institutions
Research Institutions > Research Centres
Research Institutions > Research Centres > Bayreuth Center for Material Science and Engineering - BayMAT
Result of work at the UBT: Yes
DDC Subjects: 600 Technology, medicine, applied sciences
600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited: 15 Feb 2018 08:00
Last Modified: 15 Feb 2018 08:00
URI: https://eref.uni-bayreuth.de/id/eprint/42278