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

Sanni Voutilainen, Arja Paananen, Martina Lille, Markus B. Linder (Corresponding Author)

    Research output: Contribution to journalArticleScientificpeer-review

    4 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 Sep 2019
    MoE publication typeA1 Journal article-refereed

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