TY - JOUR
T1 - Modular protein architectures for pH-dependent interactions and switchable assembly of nanocellulose
AU - Voutilainen, Sanni
AU - Paananen, Arja
AU - Lille, Martina
AU - Linder, Markus B.
N1 - Funding Information:
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.
Publisher Copyright:
© 2019
Copyright:
Copyright 2019 Elsevier B.V., All rights reserved.
PY - 2019/9/15
Y1 - 2019/9/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85068262151&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2019.06.227
DO - 10.1016/j.ijbiomac.2019.06.227
M3 - Article
AN - SCOPUS:85068262151
SN - 0141-8130
VL - 137
SP - 270
EP - 276
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -