Controlled Hydrogel Formation of a Recombinant Spider Silk Protein

Title data

Schacht, Kristin ; Scheibel, Thomas:
Controlled Hydrogel Formation of a Recombinant Spider Silk Protein.
In: Biomacromolecules. Vol. 12 (2011) Issue 7 . - pp. 2488-2495.
ISSN 1526-4602
DOI: https://doi.org/10.1021/bm200154k

Official URL:

Abstract in another language

Due to their biocompatibility, biodegradability, and low immunogenicity, recombinant spider silk proteins have a high potential for a variety of applications when processed into morphologies such as films, capsules, beads, or hydrogels. Here, hydrogels made of the engineered and recombinantly produced spider silk protein eADF4(C16) were analyzed in detail. It has previously been shown that eADF4(C16) nanofibrils self-assemble by a mechanism of nucleation-aggregation, providing the basis of silk hydrogels. We focused on establishing a reproducible gelation process by employing different protein concentrations, chemical crosslinking, and unctionalization of eADF4(C16)with fluorescein. Fluorescein strongly influenced assembly as well as the properties of the hydrogels, such as pore sizes and mechanical behavior, possibly due to its interference with packing of silk nanofibrils during hydrogel formation.

Further data

Item Type:	Article in a journal
Refereed:	Yes
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:	01 Jul 2015 10:03
Last Modified:	22 Apr 2022 10:32
URI:	https://eref.uni-bayreuth.de/id/eprint/15594