Lehrstuhl Biomaterialien, Fakultät für Ingenieurwissenschaften, Universität Bayreuth, Universitätsstraße 30, 95440, Bayreuth, Germany.
Bayreuther Zentrum für Kolloide und Grenzflächen (BZKG), Universität Bayreuth, Universitätsstraße 30, 95440, Bayreuth, Germany.
Macromol Biosci. 2017 Nov;17(11). doi: 10.1002/mabi.201700141. Epub 2017 Aug 14.
Recombinantly produced spider silk proteins have high potential for bioengineering and various biomedical applications because of their biocompatibility, biodegradability, and low immunogenicity. Here, the recently described small spider silk protein eMaSp1s is assembled into hydrogels, which can be 3D printed into scaffolds. Further, blending with a recombinantly produced MaSp2 derivative eADF4(C16) alters the mechanical properties of the resulting hydrogels. Different spider silk hydrogels also show a distinct recovery after a high shear stress deformation, exhibiting the tunability of their features for selected applications.
重组蛛丝蛋白具有良好的生物相容性、可生物降解性和低免疫原性,因此在生物工程和各种生物医学应用中具有巨大的潜力。在这里,最近描述的小型蛛丝蛋白 eMaSp1s 被组装成水凝胶,可以 3D 打印成支架。此外,与重组 MaSp2 衍生物 eADF4(C16) 混合可以改变所得水凝胶的机械性能。不同的蜘蛛丝水凝胶在经受高剪切应变速形后也表现出明显的恢复,这表明它们的特性可以针对特定应用进行调整。