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 language | English |
|---|---|
| Pages (from-to) | 11795-11805 |
| Number of pages | 11 |
| Journal | Langmuir |
| Volume | 34 |
| Issue number | 39 |
| DOIs | |
| Publication status | Published - 5 Sep 2018 |
| MoE publication type | Not Eligible |
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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 journal › Article › Scientific › peer-review
TY - JOUR
T1 - Interfacial Behavior of Recombinant Spider Silk Protein Parts Reveals Cues on the Silk Assembly Mechanism
AU - Nilebäck, Linnea
AU - Arola, Suvi
AU - Kvick, Mathias
AU - Paananen, Arja
AU - Linder, Markus B.
AU - Hedhammar, My
PY - 2018/9/5
Y1 - 2018/9/5
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85053916732&partnerID=8YFLogxK
U2 - 10.1021/acs.langmuir.8b02381
DO - 10.1021/acs.langmuir.8b02381
M3 - Article
C2 - 30183309
AN - SCOPUS:85053916732
VL - 34
SP - 11795
EP - 11805
JO - Langmuir
JF - Langmuir
SN - 0743-7463
IS - 39
ER -