Zeng Like, Jiang Linan, Teng Weibing, Cappello Joseph, Zohar Yitshak, Wu Xiaoyi
Department of Aerospace and Mechanical Engineering, University of Arizona, Tucson, AZ, 85721, USA.
Macromol Rapid Commun. 2014 Jul;35(14):1273-9. doi: 10.1002/marc.201400058. Epub 2014 May 3.
Self-assembled peptide/protein nanofibers are valuable 1D building blocks for creating complex structures with designed properties and functions. It is reported that the self-assembly of silk-elastin-like protein polymers into nanofibers or globular aggregates in aqueous solutions can be modulated by tuning the temperature of the protein solutions, the size of the silk blocks, and the charge of the elastin blocks. A core-sheath model is proposed for nanofiber formation, with the silk blocks in the cores and the hydrated elastin blocks in the sheaths. The folding of the silk blocks into stable cores--affected by the size of the silk blocks and the charge of the elastin blocks--plays a critical role in the assembly of silk-elastin nanofibers. Furthermore, enhanced hydrophobic interactions between the elastin blocks at elevated temperatures greatly influence the nanoscale features of silk-elastin nanofibers.
自组装肽/蛋白质纳米纤维是用于构建具有设计特性和功能的复杂结构的有价值的一维构建单元。据报道，在水溶液中，类丝素弹性蛋白聚合物自组装成纳米纤维或球状聚集体的过程可以通过调节蛋白质溶液的温度、丝素嵌段的大小以及弹性蛋白嵌段的电荷来调控。针对纳米纤维的形成提出了一种核壳模型，其中丝素嵌段位于核中，水合弹性蛋白嵌段位于壳中。丝素嵌段折叠成稳定的核——受丝素嵌段大小和弹性蛋白嵌段电荷的影响——在丝素弹性蛋白纳米纤维的组装中起着关键作用。此外，在升高的温度下弹性蛋白嵌段之间增强的疏水相互作用极大地影响了丝素弹性蛋白纳米纤维的纳米级特征。
