Modular protein architectures for pH-dependent interactions and switchable assembly of nanocellulose

Sanni Voutilainen, Arja Paananen, Martina Lille, Markus B. Linder*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

7 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)270-276
JournalInternational Journal of Biological Macromolecules
Volume137
Early online date29 Jun 2019
DOIs
Publication statusPublished - 15 Sept 2019
MoE publication typeA1 Journal article-refereed

Funding

The work was performed within the Academy of Finland Center of Excellence Programme (2014-2019) and Academy of Finland projects 307474, 317395 and 317019. We are grateful for the support by the FinnCERES Materials Bioeconomy Ecosystem.

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