Xu Chunyu, Breedveld Victor, Kopecek Jindrich
Department of Pharmaceutics and Pharmaceutical Chemistry and of Bioengineering, University of Utah, Salt Lake City, Utah 84112, USA.
Biomacromolecules. 2005 May-Jun;6(3):1739-49. doi: 10.1021/bm050017f.
A series of triblock protein copolymers composed of a central water-soluble polyelectrolyte segment flanked by two coiled-coil domains was synthesized by genetic engineering methods. The copolymers self-assembled into reversible hydrogels in response to changes in temperature, pH, and the presence or absence of denaturating agent (guanidine hydrochloride, GdnHCl). Hydrogel formation was concentration-dependent, and the concentration needed for hydrogel formation correlated with the oligomerization state of the coiled-coil domains in the protein copolymers. The morphology of the hydrogels, as determined by scanning electron microscopy (SEM), indicated the presence of porous interconnected networks. The thermal stabilities and self-assembling properties of the protein copolymers were successfully controlled by manipulating the amino acid sequences of the coiled-coil domains. The stimuli responsiveness and reversibility of the hydrogel self-assembly suggest that these protein copolymers may have potential in biomedical applications.
通过基因工程方法合成了一系列三嵌段蛋白质共聚物，其由位于中央的水溶性聚电解质链段和两侧的两个卷曲螺旋结构域组成。这些共聚物会根据温度、pH值以及变性剂（盐酸胍，GdnHCl）的存在与否发生自组装，形成可逆水凝胶。水凝胶的形成具有浓度依赖性，形成水凝胶所需的浓度与蛋白质共聚物中卷曲螺旋结构域的寡聚化状态相关。通过扫描电子显微镜（SEM）测定的水凝胶形态表明存在多孔互连网络。通过操纵卷曲螺旋结构域的氨基酸序列，成功控制了蛋白质共聚物的热稳定性和自组装特性。水凝胶自组装的刺激响应性和可逆性表明，这些蛋白质共聚物在生物医学应用中可能具有潜力。
