Dissertation/Thesis Abstract

Herstellung und Charakterisierung Artifizieller Assemblierungsmorphologien und Komposit-Materialien aus Rekombinanten Spinnenseidenproteinen
by Doblhofer, Elena, Dr.Nat., Universitaet Bayreuth (Germany), 2016, 166; 11005788
Abstract (Summary)

Over the last few decades, plastics made of synthetic polymers were in the focus of scientific research and their use resulted in enormous medical and technical advances of mankind. However, shortly after industrial production of plastics, negative influences of this material on nature became apparent: Plastic fragments were found in perished sea birds and micro plastic was spotted in remote marine habitats. These occurrences and the consequences thereof encouraged scientists to look for non-petrochemical and biodegradable materials which can still be used in a great variety of applications. One class of material that can be used as a substitute for synthetic polymers is the class of proteins. Protein materials are biodegradable and provide a large variety of functional groups for modification. In contrast to most other proteins, recombinantly produced spider silk proteins offer the possibility for modification of the primary structure as well as high purity, due to their biotechnological production. Recombinant spider silk proteins, furthermore, have low-immunogenicity, are non-toxic and morphologies made of these proteins exhibit high mechanical stability. Recently, the anionic recombinant spider silk protein eADF4(C16) was designed based on the repetitive core of the natural spider silk protein ADF4 (Araneus diadematus fibroin 4) which can be found in the dragline silk of the European garden spider. Due to its negative net charge eADF4(C16) is especially suitable for applications in which good interactions with positively charged substances, as well as no interactions between cells and protein surfaces are required. For an extended application range of recombinant spider silk proteins, this work focused on the development of a new and positively charged variant of eADF4 and its medical and technical applications. Therefore, every codon for L-glutamic acid (negatively charged at pH 7) of in the DNA template of eADF4(C16) was exchanged by a codon for L-lysine (positively charged at pH 7). The resulting protein was named eADF4(ΔΈ16) and exhibits 16 positive net charges. After successful production and purification, this protein was tested for its possible applications in two different assembly morphologies.

Indexing (document details)
School: Universitaet Bayreuth (Germany)
School Location: Germany
Source: DAI-C 81/1(E), Dissertation Abstracts International
Subjects: Bioengineering, Materials science, Plastics
Keywords: Recombinant spider silk proteins
Publication Number: 11005788
ISBN: 9781088397831
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