Interfacial Behavior of Recombinant Spider Silk Protein Parts Reveals Cues on the Silk Assembly Mechanism

Research output: Contribution to journalArticleScientificpeer-review

Researchers

  • Linnea Nilebäck
  • Suvi Arola
  • Mathias Kvick
  • Arja Paananen
  • Markus Linder

  • My Hedhammar

Research units

  • Royal Institute of Technology
  • VTT Technical Research Centre of Finland

Abstract

The mechanism of silk assembly, and thus the cues for the extraordinary properties of silk, can be explored by studying the simplest protein parts needed for the formation of silk-like materials. The recombinant spider silk protein 4RepCT, consisting of four repeats of polyalanine and glycine-rich segments (4Rep) and a globular C-terminal domain (CT), has previously been shown to assemble into silk-like fibers at the liquid-air interface. Herein, we study the interfacial behavior of the two parts of 4RepCT, revealing new details on how each protein part is crucial for the silk assembly. Interfacial rheology and quartz crystal microbalance with dissipation show that 4Rep interacts readily at the interfaces. However, organized nanofibrillar structures are formed only when 4Rep is fused to CT. A strong interplay between the parts to direct the assembly is demonstrated. The presence of either a liquid-air or a liquid-solid interface had a surprisingly similar influence on the assembly.

Details

Original languageEnglish
Pages (from-to)11795–11805
JournalLangmuir
Volume34
Issue number39
Publication statusPublished - 5 Sep 2018
MoE publication typeA1 Journal article-refereed

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