预拉伸对丝蛋白力学性能影响的全原子网络模型

Translated title of the contribution: An atomistic model of silk protein network for studying the effect of pre-stretching on the mechanical performances of silks

Wenhui Shen, Zihan Tang, Xuwei Wu, Liang Pan, Yuan Cheng, Bo Huo, Jizhou Song, Weiqiu Chen, Baohua Ji, Dechang Li

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Silk protein builds one of the strongest natural fibers based on its complex nanocomposite structures. However, the mechanical performance of silk protein, related to its molecular structure and packing is still elusive. In this study, we constructed an atomistic silk protein network model, which reproduces the extensive connection topology of silk protein with structure details of the β-sheet crystallites and amorphous domains. With the silk protein network model, we investigated the structure evolution and stress distribution of silk protein under external loading. We found a pre-stretching treatment during the spinning process can improve the strength of silk protein. This treatment improves the properties of silk protein network, i.e., increases the number of nodes and bridges, makes the nodes distributed homogeneously, and induces the bridges in the network well aligned to the loading direction, which is of great benefit to the mechanical performances of silk protein. Our study not only provides a realized atomistic model for silk protein network that well represents the structures and deformations of silk proteins under loading, but also gains deep insights into the mechanism how the pre-loading on silk proteins during spinning improves the mechanical properties of silk fibers.

Translated title of the contributionAn atomistic model of silk protein network for studying the effect of pre-stretching on the mechanical performances of silks
Original languageMandarin
Article number222013
Number of pages14
JournalActa Mechanica Sinica/Lixue Xuebao
Volume38
Issue number6
DOIs
Publication statusPublished - 24 Mar 2022

Keywords

  • Amorphous domain
  • Mechanical performances
  • Molecular dynamics
  • Silk protein
  • β-sheet crystallite

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