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潮湿蜘蛛丝纤维中应变依赖性分数分子扩散

Strain-dependent fractional molecular diffusion in humid spider silk fibres.

作者信息

Krasnov Igor, Seydel Tilo, Greving Imke, Blankenburg Malte, Vollrath Fritz, Müller Martin

机构信息

Institut für Experimentelle und Angewandte Physik, Universität Kiel, 24098 Kiel, Germany Institute of Materials Research, Helmholtz-Zentrum Geesthacht (HZG), 21502 Geesthacht, Germany.

Institut Max von Laue-Paul Langevin (ILL), CS 20156, 38042 Grenoble, France

出版信息

J R Soc Interface. 2016 Sep;13(122). doi: 10.1098/rsif.2016.0506.

DOI:10.1098/rsif.2016.0506
PMID:27628174
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5046950/
Abstract

Spider silk is a material well known for its outstanding mechanical properties, combining elasticity and tensile strength. The molecular mobility within the silk's polymer structure on the nanometre length scale importantly contributes to these macroscopic properties. We have therefore investigated the ensemble-averaged single-particle self-dynamics of the prevailing hydrogen atoms in humid spider dragline silk fibres on picosecond time scales in situ as a function of an externally applied tensile strain. We find that the molecular diffusion in the amorphous fraction of the oriented fibres can be described by a generalized fractional diffusion coefficient Kα that is independent of the observation length scale in the probed range from approximately 0.3-3.5 nm. Kα increases towards a diffusion coefficient of the classical Fickian type with increasing tensile strain consistent with an increasing loss of memory or entropy in the polymer matrix.

摘要

蜘蛛丝是一种以其出色的机械性能而闻名的材料,兼具弹性和拉伸强度。丝聚合物结构内纳米长度尺度上的分子运动性对这些宏观性能起着重要作用。因此,我们研究了在皮秒时间尺度上,作为外部施加拉伸应变的函数,潮湿蜘蛛拖丝纤维中主要氢原子的系综平均单粒子自动力学。我们发现,取向纤维非晶部分的分子扩散可以用一个广义分数扩散系数Kα来描述,该系数在约0.3 - 3.5纳米的探测范围内与观测长度尺度无关。随着拉伸应变的增加,Kα朝着经典菲克型扩散系数增加,这与聚合物基质中记忆或熵的损失增加一致。

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本文引用的文献

1
Spider silk as archetypal protein elastomer.蜘蛛丝作为典型的蛋白质弹性体。
Soft Matter. 2006 Apr 18;2(5):377-385. doi: 10.1039/b600098n.
2
Elasticity and Inverse Temperature Transition in Elastin.弹性蛋白中的弹性与逆温度转变
J Phys Chem Lett. 2015 Oct 15;6(20):4018-25. doi: 10.1021/acs.jpclett.5b01890. Epub 2015 Sep 24.
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Fractional dynamics in silk: From molecular picosecond subdiffusion to macroscopic long-time relaxation.丝绸中的分数动力学:从分子皮秒亚扩散到宏观长时间弛豫。
Phys Rev E Stat Nonlin Soft Matter Phys. 2015 Apr;91(4):042716. doi: 10.1103/PhysRevE.91.042716. Epub 2015 Apr 28.
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Spider silk: super material or thin fibre?蜘蛛丝:超级材料还是细纤维?
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The critical role of water in spider silk and its consequence for protein mechanics.水在蜘蛛丝中的关键作用及其对蛋白质力学的影响。
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Increased molecular mobility in humid silk fibers under tensile stress.拉伸应力下湿态丝纤维中分子流动性增加。
Phys Rev E Stat Nonlin Soft Matter Phys. 2011 Jan;83(1 Pt 2):016104. doi: 10.1103/PhysRevE.83.016104. Epub 2011 Jan 13.
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Nanostructure and molecular mechanics of spider dragline silk protein assemblies.蜘蛛牵引丝蛋白组装体的纳米结构和分子力学。
J R Soc Interface. 2010 Dec 6;7(53):1709-21. doi: 10.1098/rsif.2010.0149. Epub 2010 Jun 2.
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Molecular and nanostructural mechanisms of deformation, strength and toughness of spider silk fibrils.蜘蛛丝纤维变形、强度和韧性的分子及纳米结构机制。
Nano Lett. 2010 Jul 14;10(7):2626-34. doi: 10.1021/nl101341w.
9
Spider silk as a novel high performance biomimetic muscle driven by humidity.蜘蛛丝作为一种由湿度驱动的新型高性能仿生肌肉。
J Exp Biol. 2009 Jul;212(Pt 13):1990-4. doi: 10.1242/jeb.028282.
10
How super is supercontraction? Persistent versus cyclic responses to humidity in spider dragline silk.超级收缩有多“超级”?蜘蛛拖网丝对湿度的持续与周期性反应。
J Exp Biol. 2009 Jul;212(Pt 13):1981-9. doi: 10.1242/jeb.028944.