Monolayer wall nanotubes self-assembled from short peptide bolaamphiphiles

Abstract

In spite of extensive research, it remains a formidable challenge to control the dimension of the nanostructures self-assembled from short designed peptides. In this work, we show that peptide bolaamphiphiles form monolayer wall nanotubes, facilitated by the interplay between the side chain structure and hydrophobicity of the central residues. The peptide KI₄K self-assembles into nanotubes with a width of ~ 100 nm, but changes in the molecular structure of amino acid side chains could hugely impact the nanostructures formed. The three variants of KI₄K, via the substitution of aromatic amino acids (F, Y, and Dopa) for the I residue closest to the C-terminus, could substantially reduce nanotube diameters, indicating a significant steric hindrance of the benzene rings on the lateral packing of β-sheets. However, the introduction of hydroxyl groups on the benzene rings alleviates the steric effect, with nanotube diameter increasing in the order of KI₃FK, KI₃YK, and KI₃DopaK, suggesting the formation of side chain H-bonds between β-sheets in addition to hydrophobic contacts. Because the self-assembly process of KI₃DopaK nanotubes is slow, key intermediates and their structural details are well characterized. With increasing incubation time, monolayered twisted ribbons and helical ribbons grow into mature KI₃DopaK nanotubes via the pitch closing route.

Keywords: Formation pathway; Intermediate; Nanotube; Peptide bolaamphiphile; Self-assembly.