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.
Highlights
T wo-dimensional (2D) nanostructures are an important material class with diverse potential applications.[1−4] It remains a challenge to produce free-standing 2D materials without a templating surface or confined space
The hexaphenylalanine segment was incorporated to provide H-bonding to form β-sheets in the x-axial direction, with concomitant βsheet stacking in the y-axial direction via aromatic interactions (Figure 1b).[24−26,29,30] The resulting self-assembly in 2D is consistent with previous studies where tyrosine and phenylalanine-rich peptides have been reported to form 2D nanobelts and nanosheets.[20,29]
The aggregation of F6C11 was confirmed by Nile Red fluorescence, where an increase of emission intensity and a spectral blue shift was observed, indicating the solubilization of Nile Red in a hydrophobic domain (Figure 1c)
Summary
T wo-dimensional (2D) nanostructures are an important material class with diverse potential applications.[1−4] It remains a challenge to produce free-standing 2D materials without a templating surface or confined space. The ThT assay confirmed the existence of rigid β-sheets with an increase of fluorescence emission in nanosheets (Figure S5). The surface of the nanosheets can selectively display specific reactive groups via coassembly of F6C11 and functionalized peptides that share the same backbone (Figure S1).
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
