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.

Functionalization of Recombinant Amelogenin Nanospheres Allows Their Binding to Cellulose Materials

“…Additionally, existence of nano‐ and microcrystalline forms can further extend the potential uses of cellulose . Immobilization of protein molecules on cellulose materials have previously been used to create protein/cellulose composites with new functionalities and distinct properties . Combining amelogenin with cellulose could be one way to create new formulations of amelogenin for clinical use, such as new types of wound dressings.…”

Modular genetic design of multi-domain functional amyloids: insights into self-assembly and functional properties

“…This slight distortion in intersheet packing distance could be attributed to the stress exerted on the amyloid backbone by the fused domains. 6,18,35 Collectively, these observations thus suggest that fusion of one or two functional domains at varied positions slows down bril assembly and affect bril morphology, but does not disrupt amyloid assembly or the typical cross-beta bril structures of CsgA.…”

“…The engineering of articial protein-based molecular materials that mimic or even outperform their natural counterparts may become feasible by rationally designing tailored molecular sequences using a bottom-up modular genetic strategy. [4][5][6] Such a research strategy represents new opportunities for engineering multifunctional molecular materials with predictable structures and customizable performance. 7 Although originally identied as pathological hallmarks of diverse neurological disorders including Alzheimer's, Parkinson's, and Huntington's diseases, 8,9 amyloids of diverse sequences have been recently identied in several organisms for physiological applications.…”

“…10,[12][13][14][15][16][17] However, genetically modied amyloids created through this strategy do not always self-assemble into "normal" structures with predictable functions. 6,18 For example, Forman et al revealed that the conformation and position of proteins displayed on the same amyloidogenic cores signicantly changed the morphology of the assembled brils. 18 The increasing development and application of such self-assembling molecular materials, therefore, call for deeper understanding of how genetically fused domains affect the stability, morphology, assembly kinetics, mechanical and functional properties of structural amyloids.…”

Self-assembled hydrophobin for producing water-soluble and membrane permeable fluorescent dye

“…Hydrophobin are a novel type of amphiphilic small proteins produced by the filamentous fungi, which are characterized for their self-assembling into protein films on different hydrophobic/hydrophilic surfaces to modify their surface properties 19 . The ability of hydrophobin to convert hydrophobic surfaces to hydrophilic ones has been documented in several studies 20 21 22 23 24 . Considering the properties of hydrophobin, we proposed that hydrophobin might alter the hydrophobicity of fluorescent dyes to improve their abilities of solubility and membrane permeability.…”