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Department of Materials, Department of Bioengineering and Institute of Biomedical Engineering, Imperial College London, Exhibition Road, London SW7 2AZ, U.K.
Published: October 2017
AI Article Synopsis
* The assembling process utilizes the interaction between peptide β-strands and hydrocarbon chains to form Janus structures, which have distinct functional surfaces.
* By fine-tuning intermolecular forces, we transitioned these 2D nanosheets into a 1D form, allowing for improved engineering of other components like proteins or nanoparticles, leading to better enzyme performance.
Article Abstract
We report the thermodynamically controlled growth of solution-processable and free-standing nanosheets via peptide assembly in two dimensions. By taking advantage of self-sorting between peptide β-strands and hydrocarbon chains, we have demonstrated the formation of Janus 2D structures with single-layer thickness, which enable a predetermined surface heterofunctionalization. A controlled 2D-to-1D morphological transition was achieved by subtly adjusting the intermolecular forces. These nanosheets provide an ideal substrate for the engineering of guest components (e.g., proteins and nanoparticles), where enhanced enzyme activity was observed. We anticipate that sequence-specific programmed peptides will offer promise as design elements for 2D assemblies with face-selective functionalization.
