Supramolecular Self‐Assembly of β³‐Peptides Mediated by Janus‐Type Recognition Units

Abstract

To gain mechanistic insights, natural systems with biochemical relevance are inspiring for the creation of new biomimetics with unique properties and functions. Despite progress in rational design and protein engineering, folding and intramolecular organization of individual components into supramolecular structures remains challenging and requires controlled methods. Foldamers, such as β‐peptides, are structurally well defined with rigid conformations and suitable for the specific arrangement of recognition units. Herein, we show the molecular arrangement and aggregation of β3‐peptides into a hexameric helix bundle. For this purpose, β‐amino acid side chains were modified with cyanuric acid and triamino‐s‐triazine as complementary recognition units. The pre‐organization of the β3‐peptides leads these Janus molecule pairs into a hexameric arrangement and a defined rosette nanotube by stacking. The helical conformation of the subunits was indicated by circular dichroism spectroscopy, while the supramolecular arrangement was detected by dynamic light scattering and confirmed by high‐resolution electrospray ionization mass spectrometry (ESI‐HRMS).

Transmembrane β‐peptide helices as molecular rulers at the membrane surface

“…In general, β-peptides are derived from α-amino acids containing an additional methylene unit compared with α-amino acids. [14][15][16][17][18][19][20][21] Depending on the position and configuration of the side chains, β-peptides yield well-defined secondary structures, with the 14-helix secondary structure being particularly valuable for the molecular ruler approach, because three amino acids per turn yield a conformationally highly stable helix with long persistence length and a 1.56 Å rise per residue.…”