title: Modular architecture of protein binding units for designing properties of cellulose nanomaterials.
abstract: Molecular biomimetic models suggest that proteins in the soft matrix of nanocomposites have a multimodular architecture. Engineered proteins were used together with nanofibrillated cellulose (NFC) to show how this type of architecture leads to function. The proteins consist of two cellulose-binding modules (CBM) separated by 12-, 24-, or 48-mer linkers. Engineering the linkers has a considerable effects on the interaction between protein and NFC in both wet colloidal state and a dry film. The protein optionally incorporates a multimerizing hydrophobin (HFB) domain connected by another linker. The modular structure explains effects in the hydrated gel state, as well as the deformation of composite materials through stress distribution and crosslinking. Based on this work, strategies can be suggested for tuning the mechanical properties of materials through the coupling of protein modules and their interlinking architectures.
authors: VTT Technical Research Centre of Finland, Tietotie 2, P.O. Box 1000, 02044 Espoo (Finland).
authors: Jani-Markus
authors: JM
authors: Malho
authors: School of Chemical Technology, Aalto University, P.O. Box 16100, 00076 Aalto (Finland).|VTT Technical Research Centre of Finland, Tietotie 2, P.O. Box 1000, 02044 Espoo (Finland).
authors: Suvi
authors: S
authors: Arola
authors: School of Chemical Technology, Aalto University, P.O. Box 16100, 00076 Aalto (Finland).
authors: Päivi
authors: P
authors: Laaksonen
authors: VTT Technical Research Centre of Finland, Tietotie 2, P.O. Box 1000, 02044 Espoo (Finland).
authors: Géza R
authors: GR
authors: Szilvay
authors: School of Science, Aalto University, P.O. Box 15100, 00076 Aalto (Finland).
authors: Olli
authors: O
authors: Ikkala
authors: School of Chemical Technology, Aalto University, P.O. Box 16100, 00076 Aalto (Finland). markus.linder@aalto.fi.
authors: Markus B
authors: MB
authors: Linder
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D032701:Biomimetics; D002482:Cellulose / Q000737:chemistry* / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D005782:Gels / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D057139:Nanofibers / Q000737:chemistry* / Q000648:ultrastructure; D049329:Nanostructures / Q000737:chemistry*; D011485:Protein Binding; D013718:Tensile Strength; D014242:Trichoderma / Q000737:chemistry*
chemical_list: D005656:Fungal Proteins; D005782:Gels; D002482:Cellulose
keywords: biomimetics; cellulose; materials; nanocomposites; supramolecular chemistry