Bionanocomposites: Differential Effects of Cellulose Nanocrystals on Protein Diblock Copolymers
Autor: | Sandra M. Da Silva, Christoph Weder, Deng Yan, E. Johan Foster, Raymond S. Tu, J.W. Gilman, Iulia Sacui, Jin Kim Montclare, Silvana Mueller, Jennifer S. Haghpanah |
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Rok vydání: | 2013 |
Předmět: |
Polymers and Plastics
Surface Properties Mechanical integrity Biocompatible Materials Bioengineering 02 engineering and technology Cartilage Oligomeric Matrix Protein 010402 general chemistry 01 natural sciences Protein Structure Secondary Nanocomposites Biomaterials Colloid Elastic Modulus Materials Testing Polymer chemistry Materials Chemistry Copolymer Animals Colloids Urochordata Cellulose Cartilage oligomeric matrix protein Aqueous solution biology Chemistry 021001 nanoscience & nanotechnology Differential effects Peptide Fragments Elastin 0104 chemical sciences Cellulose nanocrystals Chemical engineering biology.protein Nanoparticles 0210 nano-technology Hydrophobic and Hydrophilic Interactions |
Zdroj: | BIOMACROMOLECULES |
ISSN: | 1526-4602 1525-7797 |
Popis: | We investigate the effects of mixing a colloidal suspension of tunicate-derived cellulose nanocrystals (t-CNCs) with aqueous colloidal suspensions of two protein diblock copolymers, EC and CE, which bear two different self-assembling domains (SADs) derived from elastin (E) and the coiled-coil region of cartilage oligomeric matrix protein (C). The resulting aqueous mixtures reveal improved mechanical integrity for the CE+t-CNC mixture, which exhibits an elastic gel network. This is in contrast to EC+t-CNC, which does not form a gel, indicating that block orientation influences the ability to interact with t-CNCs. Surface analysis and interfacial characterization indicate that the differential mechanical properties of the two samples are due to the prevalent display of the E domain by CE, which interacts more with t-CNCs leading to a stronger network with t-CNCs. On the other hand, EC, which is predominantly C-rich on its surface, does not interact as much with t-CNCs. This suggests that the surface characteristics of the protein polymers, due to folding and self-assembly, are important factors for the interactions with t-CNCs, and a significant influence on the overall mechanical properties. These results have interesting implications for the understanding of cellulose hydrophobic interactions, natural biomaterials and the development of artificially assembled bionanocomposites. |
Databáze: | OpenAIRE |
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