Self-Assembly of Spider Silk-Fusion Proteins Comprising Enzymatic and Fluorescence Activity.
Bioconjug Chem
; 29(4): 898-904, 2018 04 18.
Article
em En
| MEDLINE
| ID: mdl-29338201
ABSTRACT
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Aranhas
/
Materiais Biocompatíveis
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Seda
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Proteínas de Artrópodes
Limite:
Animals
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article