Literatur vom gleichen Autor/der gleichen Autor*in
plus bei Google Scholar

Bibliografische Daten exportieren
 

Structure-Property Relationship Based on the Amino Acid Composition of Recombinant Spider Silk Proteins for Potential Biomedical Applications

Titelangaben

Lentz, Sarah ; Trossmann, Vanessa T. ; Borkner, Christian B. ; Beyersdorfer, Vivien ; Rottmar, Markus ; Scheibel, Thomas:
Structure-Property Relationship Based on the Amino Acid Composition of Recombinant Spider Silk Proteins for Potential Biomedical Applications.
In: ACS Applied Materials & Interfaces. Bd. 14 (2022) Heft 28 . - S. 31751-31766.
ISSN 1944-8252
DOI: https://doi.org/10.1021/acsami.2c09590

Volltext

Link zum Volltext (externe URL): Volltext

Angaben zu Projekten

Projektfinanzierung: Deutsche Forschungsgemeinschaft

Abstract

Improving biomaterials by engineering application-specific and adjustable properties is of increasing interest. Most of the commonly available materials fulfill the mechanical and physical requirements of relevant biomedical applications, but they lack biological functionality, including biocompatibility and prevention of microbial infestation. Thus, research has focused on customizable, application-specific, and modifiable surface coatings to cope with the limitations of existing biomaterials. In the case of adjustable degradation and configurable interaction with body fluids and cells, these coatings enlarge the applicability of the underlying biomaterials. Silks are interesting coating materials, e.g., for implants, since they exhibit excellent biocompatibility and mechanical properties. Herein, we present putative implant coatings made of five engineered recombinant spider silk proteins derived from the European garden spider Araneus diadematus fibroins (ADF), differing in amino acid sequence and charge. We analyzed the influence of the underlying amino acid composition on wetting behavior, blood compatibility, biodegradability, serum protein adsorption, and cell adhesion. The outcome of the comparison indicates that spider silk coatings can be engineered for explicit biomedical applications.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Keywords: recombinant spider silk proteins; blood coagulation; enzymatic degradation; cell adhesion; protein adsorption; surface properties
Institutionen der Universität: Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien > Lehrstuhl Biomaterialien - Univ.-Prof. Dr. Thomas Scheibel
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 600 Technik, Medizin, angewandte Wissenschaften > 620 Ingenieurwissenschaften
Eingestellt am: 21 Dec 2023 06:37
Letzte Änderung: 21 Dec 2023 06:37
URI: https://eref.uni-bayreuth.de/id/eprint/88113