Issue 48, 2023

Self-assembly of cyclic peptide monolayers by hydrophobic supramolecular hinges

Abstract

Supramolecular polymerisation of two-dimensional (2D) materials requires monomers with non-covalent binding motifs that can control the directionality of both dimensions of growth. A tug of war between these propagation forces can bias polymerisation in either direction, ultimately determining the structure and properties of the final 2D ensemble. Deconvolution of the assembly dynamics of 2D supramolecular systems has been widely overlooked, making monomer design largely empirical. It is thus key to define new design principles for suitable monomers that allow the control of the direction and the dynamics of two-dimensional self-assembled architectures. Here, we investigate the sequential assembly mechanism of new monolayer architectures of cyclic peptide nanotubes by computational simulations and synthesised peptide sequences with selected mutations. Rationally designed cyclic peptide scaffolds are shown to undergo hierarchical self-assembly and afford monolayers of supramolecular nanotubes. The particular geometry, the rigidity and the planar conformation of cyclic peptides of alternating chirality allow the orthogonal orientation of hydrophobic domains that define lateral supramolecular contacts, and ultimately direct the propagation of the monolayers of peptide nanotubes. A flexible ‘tryptophan hinge’ at the hydrophobic interface was found to allow lateral dynamic interactions between cyclic peptides and thus maintain the stability of the tubular monolayer structure. These results unfold the potential of cyclic peptide scaffolds for the rational design of supramolecular polymerisation processes and hierarchical self-assembly across the different dimensions of space.

Graphical abstract: Self-assembly of cyclic peptide monolayers by hydrophobic supramolecular hinges

Supplementary files

Article information

Article type
Edge Article
Submitted
29 iyl 2023
Accepted
26 okt 2023
First published
27 okt 2023
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2023,14, 14074-14081

Self-assembly of cyclic peptide monolayers by hydrophobic supramolecular hinges

I. Insua, A. Cardellini, S. Díaz, J. Bergueiro, R. Capelli, G. M. Pavan and J. Montenegro, Chem. Sci., 2023, 14, 14074 DOI: 10.1039/D3SC03930G

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