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Enzymatic degradation of films, particles and non-woven meshes made of a recombinant spider silk protein

Title data

Müller-Herrmann, Susanne ; Scheibel, Thomas:
Enzymatic degradation of films, particles and non-woven meshes made of a recombinant spider silk protein.
In: ACS Biomaterials Science & Engineering. Vol. 1 (13 April 2015) Issue 4 . - pp. 247-259.
ISSN 2373-9878
DOI: https://doi.org/10.1021/ab500147u

Official URL: Volltext

Abstract in another language

The performance of biomaterials in vivo is largely influenced by their stability and the rate and extent to which they degrade. Materials for tissue engineering applications, for example, have to be mechanically stable to support cell adhesion and proliferation without collapsing. On the other hand they need to be replaced gradually by native extracellular matrix and have to be (slowly) biodegradable. Therefore, it is of critical importance to be able to tune the degradation behavior of a biomaterial. Recombinantly produced spider silk proteins have been shown to be versatile biopolymers for medical applications. They can be processed into a variety of morphologies, and by chemical or genetic modification the properties can be adjusted to specific demands. Furthermore, in vivo experiments confirmed the lack of immunological reactions towards certain spider silks. In this study the degradation behavior of the recombinant spider silk protein eADF4(C16) in solution as well as processed into particles, films and non-woven meshes was analyzed, and the impact of crosslinking of the scaffolds was assessed thereon. In addition to two bacterial proteolytic model enzymes, protease type XIV from Streptomyces griseus (PXIV) and collagenase type IA from Clostridium histolyticum (CHC) used in all experiments, several recombinant human matrix metalloproteinases (MMPs) and one elastase were used in studying degradation of soluble eADF4(C16). For soluble eADF4(C16) all degradation kinetics were similar. In case of eADF4(C16) scaffolds significant differences were observable between PXIV and CHC. All scaffolds were more stable towards proteolytic degradation in the presence of CHC than in the presence of PXIV. Further, particles were degraded significantly faster than films, and non-woven meshes showed the highest proteolytic stability. Chemical crosslinking of the scaffolds led to a decrease in both degradation rate and extent.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: Der Artikel wurde zunächst online veröffentlicht.
Keywords: recombinant silk proteins, crosslinking, biodegradation, MMPs, protease XIV, collagenase IA, scaffolds for biomedical applications
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 > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Emerging Fields > Food and Health Sciences
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Emerging Fields
Result of work at the UBT: Yes
DDC Subjects: 600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited: 10 Mar 2015 13:01
Last Modified: 26 Nov 2015 10:51
URI: https://eref.uni-bayreuth.de/id/eprint/7982