Department of Chemical and Biological Sciences, Polytechnic Institute of NYU, Brooklyn, New York 11201, United States.
Biomacromolecules. 2011 Dec 12;12(12):4240-6. doi: 10.1021/bm201083d. Epub 2011 Nov 7.
We have generated protein block polymer E(n)C and CE(n) libraries composed of two different self-assembling domains (SADs) derived from elastin (E) and the cartilage oligomeric matrix protein coiled-coil (C). As the E domain is shortened, the polymers exhibit an increase in inverse transition temperature (T(t)); however, the range of temperature change differs dramatically between the E(n)C and CE(n) library. Whereas all polymers assemble into nanoparticles, the bulk mechanical properties of the E(n)C are very different from CE(n). The E(n)C members demonstrate viscolelastic behavior under ambient conditions and assemble into elastic soft gels above their T(t) values. By contrast, the CE(n) members are predominantly viscous at all temperatures. All library members demonstrate binding to curcumin. The differential thermoresponsive behaviors of the E(n)C and CE(n) libraries in addition to their small molecule recognition abilities make them suitable for potential use in tissue engineering and drug delivery.
我们生成了由两个不同的自组装结构域（SAD）组成的蛋白嵌段聚合物 E(n)C 和 CE(n) 文库，这两个 SAD 分别来自弹性蛋白（E）和软骨寡聚基质蛋白卷曲螺旋（C）。随着 E 结构域的缩短，聚合物表现出反转变温度（T(t)）的增加；然而，E(n)C 和 CE(n) 文库之间的温度变化范围差异很大。虽然所有聚合物都组装成纳米颗粒，但 E(n)C 的体力学性质与 CE(n) 非常不同。E(n)C 成员在环境条件下表现出粘弹性行为，并在其 T(t) 值以上组装成弹性软凝胶。相比之下，CE(n) 成员在所有温度下主要表现为粘性。所有文库成员都表现出与姜黄素的结合。E(n)C 和 CE(n) 文库的差异热响应行为以及它们对小分子的识别能力使它们适合于组织工程和药物输送的潜在用途。
