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

Linnea Nilebäck, Suvi Arola, Mathias Kvick, Arja Paananen, Markus B. Linder (Corresponding Author), My Hedhammar

Research output: Contribution to journalArticleScientificpeer-review

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)11795-11805
Number of pages11
JournalLangmuir
Volume34
Issue number39
DOIs
Publication statusPublished - 5 Sep 2018
MoE publication typeNot Eligible

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spiders
silk
Silk
cues
assembly
proteins
Proteins
liquid air
Liquids
Quartz crystal microbalances
liquid-solid interfaces
glycine
Air
quartz crystals
Rheology
rheology
microbalances
Glycine
Amino acids
dissipation

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Nilebäck, Linnea ; Arola, Suvi ; Kvick, Mathias ; Paananen, Arja ; Linder, Markus B. ; Hedhammar, My. / Interfacial Behavior of Recombinant Spider Silk Protein Parts Reveals Cues on the Silk Assembly Mechanism. In: Langmuir. 2018 ; Vol. 34, No. 39. pp. 11795-11805.
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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.",
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Interfacial Behavior of Recombinant Spider Silk Protein Parts Reveals Cues on the Silk Assembly Mechanism. / Nilebäck, Linnea; Arola, Suvi; Kvick, Mathias; Paananen, Arja; Linder, Markus B. (Corresponding Author); Hedhammar, My.

In: Langmuir, Vol. 34, No. 39, 05.09.2018, p. 11795-11805.

Research output: Contribution to journalArticleScientificpeer-review

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