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Self-Assembly of an α-Helical Peptide into a Crystalline Two-Dimensional Nanoporous Framework
- Magnotti, Elizabeth L., Hughes, Spencer A., Dillard, Rebecca S., Wang, Shengyuan, Hough, Lillian, Karumbamkandathil, Arshad, Lian, Tianquan, Wall, Joseph S., Zuo, Xiaobing, Wright, Elizabeth R., Conticello, Vincent P.
- Journal of the American Chemical Society 2016 v.138 no.50 pp. 16274-16282
- amino acid sequences, models, nanofibers, nanopores, nanosheets, nanotubes, peptides, transmission electron microscopy
- Sequence-specific peptides have been demonstrated to self-assemble into structurally defined nanoscale objects including nanofibers, nanotubes, and nanosheets. The latter structures display significant promise for the construction of hybrid materials for functional devices due to their extended planar geometry. Realization of this objective necessitates the ability to control the structural features of the resultant assemblies through the peptide sequence. The design of a amphiphilic peptide, 3FD-IL, is described that comprises two repeats of a canonical 18 amino acid sequence associated with straight α-helical structures. Peptide 3FD-IL displays 3-fold screw symmetry in a helical conformation and self-assembles into nanosheets based on hexagonal packing of helices. Biophysical evidence from TEM, cryo-TEM, SAXS, AFM, and STEM measurements on the 3FD-IL nanosheets support a structural model based on a honeycomb lattice, in which the length of the peptide determines the thickness of the nanosheet and the packing of helices defines the presence of nanoscale channels that permeate the sheet. The honeycomb structure can be rationalized on the basis of geometrical packing frustration in which the channels occupy defect sites that define a periodic superlattice. The resultant 2D materials may have potential as materials for nanoscale transport and controlled release applications.