Unfolding the multi-length scale domain structure of silk fibroin protein
Unfolding the multi-length scale domain structure of silk fibroin protein
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DOI：
10.1016/j.polymer.2006.06.002
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发表时间：
2006-07-26
期刊：
影响因子：
4.6
通讯作者：
Tsukruk, Vladirnir V.
中科院分区：
文献类型：
--
作者：
Shulha, Hennady;Foo, Cheryl Wong Po;Tsukruk, Vladirnir V.
利用多尺度力谱技术研究了桑蚕丝素蛋白的去折叠特性和内部结构。我们证明，复杂的多结构域序列和块设计在这种蛋白质可以直接相关的特定区域的多阶段展开行为，通过使用力延伸测量。这些新的发现表明聚合物嵌段化学和机械特性之间的关系，作为天然丝纤维的显着机械性能的起源一般。我们观察到多个相应的展开的亲水性和疏水性结构域的特性，可以直接相关的已知分子尺寸的蛋白质骨架。可以设想未来的筛选和选择方法，以利用这种方法来优化与序列化学有关的生物聚合物和合成聚合物的特定材料功能特征，这是目前尚不具备的能力。(c)2006爱思唯尔有限公司保留所有权利。
Multi-scale force spectroscopy was applied to measure unfolding properties and the internal domain structure of Bombyx mori silk fibroin. We demonstrated that the complex multi-domain sequence and block design in this protein can be directly related to multi-stage unfolding behavior of the specific regions through the use of force extension measurements. These new findings suggest relationships between polymer block chemistry and mechanical features, as origins of the remarkable mechanical properties of native silk fibers in general. We observed multiple consequential unfolding of hydrophilic and hydrophobic domains with characteristics that can be directly related to known molecular dimensions of the protein backbones. Future screening and selection approaches can be envisioned to exploit this approach to optimize specific material functional features for both biopolymers and synthetic polymers in relation to sequence chemistry, a capability not currently available. (c) 2006 Elsevier Ltd. All rights reserved.