Functionalized DNA-spider silk nanohydrogels for controlled protein binding and release
Hydrogels are excellent scaffolds to accommodate sensitive enzymes in a protective environment. However, the lack of suitable immobilization techniques on substrates and the lack of selectivity to anchor a biocatalyst are major drawbacks preventing the use of hydrogels in bioanalytical devices. Here...
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| Format: | Article |
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Elsevier
2020-03-01
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| Series: | Materials Today Bio |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590006420300053 |
| _version_ | 1828515469500350464 |
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| author | Martin Humenik Tamara Preiß Sebastian Gödrich Georg Papastavrou Thomas Scheibel |
| author_facet | Martin Humenik Tamara Preiß Sebastian Gödrich Georg Papastavrou Thomas Scheibel |
| author_sort | Martin Humenik |
| collection | DOAJ |
| description | Hydrogels are excellent scaffolds to accommodate sensitive enzymes in a protective environment. However, the lack of suitable immobilization techniques on substrates and the lack of selectivity to anchor a biocatalyst are major drawbacks preventing the use of hydrogels in bioanalytical devices. Here, nanofilm coatings on surfaces were made of a recombinant spider silk protein (rssp) to induce rssp self-assembly and thus the formation of fibril-based nanohydrogels. To functionalize spider silk nanohydrogels for bioselective binding of proteins, two different antithrombin aptamers were chemically conjugated with the rssp, thereby integrating the target-binding function into the nanohydrogel network. Human thrombin was selected as a sensitive model target, in which the structural integrity determines its activity. The chosen aptamers, which bind various exosites of thrombin, enabled selective and cooperative embedding of the protein into the nanohydrogels. The change of the aptamer secondary structure using complementary DNA sequences led to the release of active thrombin and confirmed the addressable functionalization of spider silk nanohydrogels. |
| first_indexed | 2024-12-11T18:13:30Z |
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| id | doaj.art-8f4f92da48444d2a9310d927fe0b5988 |
| institution | Directory Open Access Journal |
| issn | 2590-0064 |
| language | English |
| last_indexed | 2024-12-11T18:13:30Z |
| publishDate | 2020-03-01 |
| publisher | Elsevier |
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| series | Materials Today Bio |
| spelling | doaj.art-8f4f92da48444d2a9310d927fe0b59882022-12-22T00:55:29ZengElsevierMaterials Today Bio2590-00642020-03-016100045Functionalized DNA-spider silk nanohydrogels for controlled protein binding and releaseMartin Humenik0Tamara Preiß1Sebastian Gödrich2Georg Papastavrou3Thomas Scheibel4Department of Biomaterials, Faculty of Engineering Science, Universität Bayreuth, Prof.-Rüdiger-Bormann.Str. 1, 95447 Bayreuth, Germany; Corresponding author.Department of Biomaterials, Faculty of Engineering Science, Universität Bayreuth, Prof.-Rüdiger-Bormann.Str. 1, 95447 Bayreuth, GermanyDepartment of Physical Chemistry II, Faculty of Biology, Chemistry & Earth Sciences, Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, GermanyDepartment of Physical Chemistry II, Faculty of Biology, Chemistry & Earth Sciences, Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany; Bayreuth Center for Colloids and Interfaces (BZKG), Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany; Bavarian Polymer Institute (BPI), Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, GermanyDepartment of Biomaterials, Faculty of Engineering Science, Universität Bayreuth, Prof.-Rüdiger-Bormann.Str. 1, 95447 Bayreuth, Germany; Bayreuth Center for Colloids and Interfaces (BZKG), Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany; Bayreuth Center for Molecular Biosciences (BZMB), Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany; Bayreuth Center for Material Science (BayMAT), Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany; Bavarian Polymer Institute (BPI), Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, GermanyHydrogels are excellent scaffolds to accommodate sensitive enzymes in a protective environment. However, the lack of suitable immobilization techniques on substrates and the lack of selectivity to anchor a biocatalyst are major drawbacks preventing the use of hydrogels in bioanalytical devices. Here, nanofilm coatings on surfaces were made of a recombinant spider silk protein (rssp) to induce rssp self-assembly and thus the formation of fibril-based nanohydrogels. To functionalize spider silk nanohydrogels for bioselective binding of proteins, two different antithrombin aptamers were chemically conjugated with the rssp, thereby integrating the target-binding function into the nanohydrogel network. Human thrombin was selected as a sensitive model target, in which the structural integrity determines its activity. The chosen aptamers, which bind various exosites of thrombin, enabled selective and cooperative embedding of the protein into the nanohydrogels. The change of the aptamer secondary structure using complementary DNA sequences led to the release of active thrombin and confirmed the addressable functionalization of spider silk nanohydrogels.http://www.sciencedirect.com/science/article/pii/S2590006420300053aptamersnanohydrogelsrecombinant spider silkself-assemblythrombin |
| spellingShingle | Martin Humenik Tamara Preiß Sebastian Gödrich Georg Papastavrou Thomas Scheibel Functionalized DNA-spider silk nanohydrogels for controlled protein binding and release Materials Today Bio aptamers nanohydrogels recombinant spider silk self-assembly thrombin |
| title | Functionalized DNA-spider silk nanohydrogels for controlled protein binding and release |
| title_full | Functionalized DNA-spider silk nanohydrogels for controlled protein binding and release |
| title_fullStr | Functionalized DNA-spider silk nanohydrogels for controlled protein binding and release |
| title_full_unstemmed | Functionalized DNA-spider silk nanohydrogels for controlled protein binding and release |
| title_short | Functionalized DNA-spider silk nanohydrogels for controlled protein binding and release |
| title_sort | functionalized dna spider silk nanohydrogels for controlled protein binding and release |
| topic | aptamers nanohydrogels recombinant spider silk self-assembly thrombin |
| url | http://www.sciencedirect.com/science/article/pii/S2590006420300053 |
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