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Tyrosine residues mediate supercontraction in biomimetic spider silk
Communications Materials Pub Date : 2021-04-12 , DOI: 10.1038/s43246-021-00147-w
Gabriele Greco , Tina Arndt , Benjamin Schmuck , Juanita Francis , Fredrik G. Bäcklund , Olga Shilkova , Andreas Barth , Nathalie Gonska , Gulaim Seisenbaeva , Vadim Kessler , Jan Johansson , Nicola M. Pugno , Anna Rising

Water and humidity severely affect the material properties of spider major ampullate silk, causing the fiber to become plasticized, contract, swell and undergo torsion. Several amino acid residue types have been proposed to be involved in this process, but the complex composition of the native fiber complicates detailed investigations. Here, we observe supercontraction in biomimetically produced artificial spider silk fibers composed of defined proteins. We found experimental evidence that proline is not the sole residue responsible for supercontraction and that tyrosine residues in the amorphous regions of the silk fiber play an important role. Furthermore, we show that the response of artificial silk fibers to humidity can be tuned, which is important for the development of materials for applications in wet environments, eg producing water resistant fibers with maximal strain at break and toughness modulus.



中文翻译:

酪氨酸残基介导仿生蜘蛛丝的超收缩

水和湿气严重影响蜘蛛主要的壶腹丝的材料性能,使纤维变塑,收缩,膨胀并发生扭曲。已经提出了几种氨基酸残基类型参与该过程,但是天然纤维的复杂组成使详细的研究复杂化。在这里,我们观察到由仿生产生的由限定蛋白质组成的人造蜘蛛丝纤维中的超收缩。我们发现实验证据表明脯氨酸不是造成超收缩的唯一残基,丝纤维无定形区域中的酪氨酸残基起着重要的作用。此外,我们证明了可以调节人造丝纤维对湿度的响应,这对于开发用于潮湿环境的材料非常重要,

更新日期:2021-04-12
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