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

Research output: Contribution to journalArticle

Researchers

Research units

  • VTT Technical Research Centre of Finland

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.

Details

Original languageEnglish
Pages (from-to)270-276
Number of pages7
JournalInternational Journal of Biological Macromolecules
Volume137
Publication statusPublished - 15 Sep 2019
MoE publication typeA1 Journal article-refereed

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