Modular architecture of protein binding units for designing properties of cellulose nanomaterials

Jani-Markus Malho, Suvi Arola, Päivi Laaksonen, Geza R. Szilvay, Olli Ikkala, Markus B. Linder (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

18 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)12025-12028
JournalAngewandte Chemie: International Edition
Volume54
Issue number41
DOIs
Publication statusPublished - 2015
MoE publication typeA1 Journal article-refereed

Fingerprint

Nanostructured materials
Cellulose
Proteins
Biomimetics
Crosslinking
Protein Binding
Stress concentration
Nanocomposites
Gels
Tuning
Mechanical properties
Composite materials

Keywords

  • biomimetics
  • cellulose
  • materials
  • nanocomposites
  • supramolecular chemistry

Cite this

Malho, Jani-Markus ; Arola, Suvi ; Laaksonen, Päivi ; Szilvay, Geza R. ; Ikkala, Olli ; Linder, Markus B. / Modular architecture of protein binding units for designing properties of cellulose nanomaterials. In: Angewandte Chemie: International Edition. 2015 ; Vol. 54, No. 41. pp. 12025-12028.
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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.",
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Modular architecture of protein binding units for designing properties of cellulose nanomaterials. / Malho, Jani-Markus; Arola, Suvi; Laaksonen, Päivi; Szilvay, Geza R.; Ikkala, Olli; Linder, Markus B. (Corresponding Author).

In: Angewandte Chemie: International Edition, Vol. 54, No. 41, 2015, p. 12025-12028.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Modular architecture of protein binding units for designing properties of cellulose nanomaterials

AU - Malho, Jani-Markus

AU - Arola, Suvi

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AU - Ikkala, Olli

AU - Linder, Markus B.

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AB - 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.

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KW - cellulose

KW - materials

KW - nanocomposites

KW - supramolecular chemistry

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