These are preliminary reports that have not been peer-reviewed. They should not be regarded as conclusive, guide clinical practice/health-related behavior, or be reported in news media as established information. For more information, please see our FAQs.
Modular protein architectures for pH-dependent interactions and switchable assembly of nanocellulose.pdf (1.63 MB)

Modular Protein Architectures for pH-Dependent Interactions and Switchable Assembly of Nanocellulose

submitted on 18.04.2019, 13:00 and posted on 19.04.2019, 16:16 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.


Academy of Finland


Email Address of Submitting Author


Aalto University



ORCID For Submitting Author


Declaration of Conflict of Interest

Declare no conflict of interest

Version Notes

version1 submitted