Lehrstuhl Biomaterialien, Fakultät Angewandte Naturwissenschaften, Universität Bayreuth, Universitätsstr. 30, 95440 Bayreuth, Germany.
Biomacromolecules. 2011 Jul 11;12(7):2488-95. doi: 10.1021/bm200154k. Epub 2011 Jun 7.
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 functionalization 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.
由于其生物相容性、可生物降解性和低免疫原性，重组蜘蛛丝蛋白在加工成薄膜、胶囊、珠粒或水凝胶等形态时，具有广泛的应用潜力。在这里，详细分析了由工程化和重组生产的蜘蛛丝蛋白 eADF4(C16)制成的水凝胶。先前已经表明，eADF4(C16)纳米原纤维通过成核-聚集的机制自组装，为丝水凝胶提供了基础。我们专注于通过使用不同的蛋白质浓度、化学交联以及用荧光素对 eADF4(C16)进行功能化，来建立可重复的凝胶化过程。荧光素强烈影响组装以及水凝胶的性质，例如孔径和机械行为，这可能是由于其在水凝胶形成过程中干扰了丝纳米原纤维的堆积。
