Conformation-driven strategy for resilient and functional protein materials.
Conformation-driven strategy for resilient and functional protein materials.
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DOI：
10.1073/pnas.2115523119
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发表时间：
2022-01-25
影响因子：
11.1
通讯作者：
Kaplan DL
中科院分区：
文献类型：
--
作者：
Mu X;Yuen JSK Jr;Choi J;Zhang Y;Cebe P;Jiang X;Zhang YS;Kaplan DL
我们深入了解对于蛋白质弹性体机械性能至关重要的序列-构象-性能关系。我们发现，仅高含量的甘氨酸残基（不包括脯氨酸）就足以实现近乎完美的弹性。脯氨酸残基的含量可能与无规卷曲的亚稳定性有关。此外，拉曼光谱作为研究构象-性质关系的有效工具，产生了半定量拉曼特征与弹性恢复幅度之间的直接相关性。此外，亚稳态构象或多态性可用于开发可表现出独特结构优点的连续机械分级的蛋白质材料。这项工作是利用天然和从头设计的蛋白质弹性体和材料序列的基础。一些蛋白质材料卓越的弹性是重要的生物力学功能的基础，在生物医学领域受到广泛关注。然而，弹性恢复力的分子设计仅限于少数天然存在的弹性蛋白（例如节肢弹性蛋白和弹性蛋白）的氨基酸序列。在这里，我们利用非弹性蛋白/弹性蛋白序列，采用动力学稳定的、随机卷曲主导的构象，以实现与弹性蛋白和弹性蛋白相媲美的近乎完美的弹性。我们还展示了弹性与拉曼表征的蛋白质构象之间的直接相关性。此外，我们证明蛋白质的亚稳态构象能够构建具有空间控制构象和弹性的机械分级蛋白质材料。这些结果提供了对蛋白质弹性体分子机制的见解，并概述了开发弹性和功能性蛋白质材料的一般构象驱动策略。
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.
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影响因子：
41.2
作者：
通讯作者：
--
影响因子：
5.8
作者：
Lim, Khoon S.;Schon, Benjamin S.;Woodfield, Tim B. F.
通讯作者：
Woodfield, Tim B. F.
DOI：
10.1073/pnas.96.11.6020
发表时间：
1999-05-25
影响因子：
11.1
作者：
Fancy, DA;Kodadek, T
通讯作者：
Kodadek, T
影响因子：
13.6
作者：
Khoury, Luai R.;Slawinski, Marina;Popa, Ionel
通讯作者：
Popa, Ionel
DOI：
10.1126/science.abd9994
发表时间：
2021-04-02
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Divine R;Dang HV;Ueda G;Fallas JA;Vulovic I;Sheffler W;Saini S;Zhao YT;Raj IX;Morawski PA;Jennewein MF;Homad LJ;Wan YH;Tooley MR;Seeger F;Etemadi A;Fahning ML;Lazarovits J;Roederer A;Walls AC;Stewart L;Mazloomi M;King NP;Campbell DJ;McGuire AT;Stamatatos L;Ruohola-Baker H;Mathieu J;Veesler D;Baker D
通讯作者：
Baker D