Conformation-driven strategy for resilient and functional protein materials
| Autor: | Xuan Mu, John Se Kit Yuen, Jaewon Choi, Yixin Zhang, Peggy Cebe, Xiaocheng Jiang, Yu Shrike Zhang, David L. Kaplan |
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| Rok vydání: | 2022 |
| Předmět: | |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.2115523119 |
| Popis: | Significance We provide insights into the sequence–conformation–property relationship that is central to the mechanical properties of protein elastomers. We find that a high content of glycine residue alone, not including proline, is sufficient for achieving near-perfect resilience. The content of proline residue may be associated with the metastability of random coils. Also, Raman spectroscopy, as a potent tool for investigating the conformation–property relationship, gives rise to a direct correlation between semiquantitative Raman features and the magnitude of elastic resilience. Moreover, metastable conformation or conformational polymorphism is useful to develop continuously and mechanically graded protein materials that may exhibit unique structural merits. This work underlies the exploitation of natural and de novo–designed sequences for protein elastomers and materials. The exceptional elastic resilience of some protein materials underlies essential biomechanical functions with broad interest in biomedical fields. However, molecular design of elastic resilience is restricted to amino acid sequences of a handful of naturally occurring resilient proteins such as resilin and elastin. Here, we exploit non-resilin/elastin sequences that adopt kinetically stabilized, random coil–dominated conformations to achieve near-perfect resilience comparable with that of resilin and elastin. We also show a direct correlation between resilience and Raman-characterized protein conformations. Furthermore, we demonstrate that metastable conformation of proteins enables the construction of mechanically graded protein materials that exhibit spatially controlled conformations and resilience. These results offer insights into molecular mechanisms of protein elastomers and outline a general conformation-driven strategy for developing resilient and functional protein materials. |
| Databáze: | OpenAIRE |
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