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Modular protein architectures for pH-dependent interactions and switchable assembly of nanocellulose.pdf (1.63 MB)
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Modular Protein Architectures for pH-Dependent Interactions and Switchable Assembly of Nanocellulose

preprint
submitted on 18.04.2019 and posted on 19.04.2019 by Sanni Voutilainen, Arja Paananen, Martina Lille, Markus Linder

Protein engineering shows a wide range of possibilities for designing properties in novel materials. Following inspiration from natural systems we have studied how combinations or duplications of protein modules can be used to engineer their interactions and achieve functional properties. Here we used cellulose binding modules (CBM) coupled to spider silk N-terminal domains that dimerize in a pH-sensitive manner. We showed how the pH-sensitive switching into dimers affected cellulose binding affinity in relation to covalent coupling between CBMs. Finally, we showed how the pH-sensitive coupling could be used to assemble cellulose nanofibers in a dynamic pH-dependent way. The work shows how novel proteins can be designed by linking functional domains from widely different sources and thereby achieve new functions in the self-assembly of nanoscale materials.

Funding

Academy of Finland

History

Email Address of Submitting Author

markus.linder@aalto.fi

Institution

Aalto University

Country

Finland

ORCID For Submitting Author

0000-0002-7271-6441

Declaration of Conflict of Interest

Declare no conflict of interest

Version Notes

version1 submitted

Exports