Department of Materials Science and Engineering, University of Delaware, Newark, Delaware 19716, United States.
Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Biomacromolecules. 2024 Apr 8;25(4):2449-2461. doi: 10.1021/acs.biomac.3c01402. Epub 2024 Mar 14.
Peptide-based materials are diverse candidates for self-assembly into modularly designed and stimuli-responsive nanostructures with precisely tunable compositions. Here, we genetically fused computationally designed coiled coil-forming peptides to the N- and C-termini of compositionally distinct multistimuli-responsive resilin-like polypeptides (RLPs) of various lengths. The successful expression of these hybrid polypeptides in bacterial hosts was confirmed through techniques such as gel electrophoresis, mass spectrometry, and amino acid analysis. Circular dichroism spectroscopy and ultraviolet-visible turbidimetry demonstrated that despite the fusion of disparate structural and responsive units, the coiled coils remained stable in the hybrid polypeptides, and the sequence-encoded differences in thermoresponsive phase separation of the RLPs were preserved. Cryogenic transmission electron microscopy and coarse-grained modeling showed that after thermal annealing in solution, the hybrid polypeptides adopted a closed loop conformation and assembled into nanofibrils capable of further hierarchically organizing into cluster structures and ribbon-like structures mediated by the self-association tendency of the RLPs.
基于肽的材料是自组装成模块化设计和刺激响应纳米结构的多样化候选物,其组成可以精确调节。在这里,我们通过基因融合的方式将计算设计的卷曲螺旋形成肽与组成不同的多刺激响应弹性蛋白样多肽(RLP)的 N 和 C 末端融合。通过凝胶电泳、质谱和氨基酸分析等技术证实了这些杂合多肽在细菌宿主中的成功表达。圆二色性光谱和紫外-可见消光法表明,尽管融合了不同的结构和响应单元,但卷曲螺旋在杂合多肽中仍然稳定,并且 RLPs 的热响应相分离的序列编码差异得以保留。低温透射电子显微镜和粗粒度建模表明,在溶液中热退火后,杂合多肽采用闭环构象,并组装成纳米纤维,这些纳米纤维能够进一步通过 RLPs 的自组装倾向组织成簇状结构和带状结构。