Self-Assembly of an α-Helical Peptide into a Crystalline Two-Dimensional Nanoporous Framework.

ABSTRACT: 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 fr

SUBMITTER: Magnotti EL 

PROVIDER: S-EPMC5739522 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature