Department of Chemistry Antonio M. Tamburrro, University of Basilicata , 85100 Potenza, Italy.
Biomacromolecules. 2011 Aug 8;12(8):2957-65. doi: 10.1021/bm2005388. Epub 2011 Jul 8.
Protein-inspired biomaterials have gained great interest as an alternative to synthetic polymers, in particular, for their potential use as biomedical devices. The potential inspiring models are mainly proteins able to confer mechanical properties to tissues and organs, such as elasticity (elastin, resilin, spider silk) and strength (collagen, silk). The proper combination of repetitive sequences, each of them derived from different proteins, represents a useful tool for obtaining biomaterials with tailored mechanical properties and biological functions. In this report we describe the design, the production, and the preliminary characterization of a chimeric polypeptide, based on sequences derived from the highly resilient proteins resilin and elastin and from collagen-like sequences. The results show that the obtained chimeric recombinant material exhibits promising self-assembling properties. Young's modulus of the fibers was determined by AFM image analysis and lies in the range of 0.1-3 MPa in agreement with the expectations for elastin-like and resilin-like materials.
蛋白质启发的生物材料作为合成聚合物的替代品引起了极大的关注，特别是因为它们作为生物医学设备的潜在用途。潜在的灵感模型主要是能够为组织和器官赋予机械性能的蛋白质，例如弹性（弹性蛋白、松弛素、蜘蛛丝）和强度（胶原蛋白、丝）。重复序列的适当组合，每个序列都来自不同的蛋白质，是获得具有定制机械性能和生物功能的生物材料的有用工具。在本报告中，我们描述了一种基于高度有弹性的蛋白质松弛素和弹性蛋白以及胶原蛋白样序列的序列设计、生产和初步表征的嵌合多肽。结果表明，所得到的嵌合重组材料表现出有前景的自组装特性。纤维的杨氏模量通过 AFM 图像分析确定，范围在 0.1-3 MPa 之间，与弹性蛋白样和松弛素样材料的预期一致。
