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
N1 - Funding Information:
*E-mail: markus.linder@aalto.fi (M.B.L.). *E-mail: myh@kth.se (M.H.). ORCID Markus B. Linder: 0000-0002-7271-6441 My Hedhammar: 0000-0003-0140-419X Author Contributions L.N. and M.H. designed and performed experiments related to the liquid−solid interface and wrote the manuscript together with M.K. All authors planned and performed experiments related to the liquid−air interface and contributed to the manuscript writing. M.K., L.N., S.A., and A.P. analyzed the data and prepared figures. All authors have given approval to the final version of the manuscript. Notes The authors declare the following competing financial interest(s): M.H. has shares in Spiber Technologies AB, a company that aims to commercialize recombinant spider silk. M.K. was funded by Spiber Technologies AB.
Funding Information:
Spiber Technologies AB is acknowledged for providing silk proteins. The authors thank Jesper Hedin and Helena Bysell for guidance related to the liquid−solid interfacial studies. FORMAS and Knut and Alice Wallenberg Foundation supported this work. The work carried out at Aalto University and VTT Ltd was supported by the Academy of Finland Center of Excellence Programme (2014−2019), the Center of Excellence in Molecular Engineering of Biosynthetic Hybrid Materials (HYBER), and Academy of Finland postdoctoral project #13311608 (2017−2020).
Publisher Copyright:
© Copyright 2018 American Chemical Society.
Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
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 -