Small-angle scattering studies on diverse peptide-based nanotube and helical ribbon structures reveal distinct form and structure factors.

Abstract

Peptide-based nanotubes are bio-based self-assembled nanostructures with intriguing structural and functional properties. The structure of such nanotubes can be probed in detail using small-angle scattering experiments due to the typical length scales, i.e. diameter and wall thickness of the nanotubes, which span the range accessible in small-angle X-ray scattering (SAXS) or small-angle neutron scattering (SANS) studies. Here, we present SAXS data for several classes of peptide and lipopeptide systems previously studied by our group, as well as newly reported data for model short lysine-sequence lipopeptides. Previous data are re-examined using more accurate models for data plotted on Kratky plots, which emphasizes fine details of nanotube structure. In some cases, consideration of structure-factor effects is necessary to allow for the coexisting structures, and a lamellar structure factor is used to describe this. In other cases, such as several examples of surfactant-like peptides, only a form factor has to be considered to accurately fit the measured SAXS data. In these cases, a form factor for hollow nanotubes with a Gaussian bilayer profile to represent the layered peptide ordering in the nanotube walls is used to model the data. A general expression for the cross section scattering form factor is provided, which can be used for any scattering density profile (electron density for SAXS or scattering length density for SANS) across the wall. This is analysed along with the form factor for multishell (multiwall) nanotube structures with a series of slabs to represent the scattering density profile. For lipopeptides C₁₆-KFK and C₁₆-K (C₁₆ indicates a hexa-decyl lipid chain), SAXS data show aperiodicity in the form-factor oscillations, as well as apparent broad structure-factor peaks. These features cannot be fitted using solely nanotube form-factor models, this being ascribed to the presence of coexisting structures. Lastly, for comparison, the form factors for helical ribbon and cochleate (scroll) structures are evaluated for several examples, since in many cases electron microscopy of peptide- and lipopeptide-based nanotube systems reveals the coexistence of nanotubes with such structures, related to nanotubes.