Themed collection Advances in supramolecular gels

These concluding remarks summarise the Faraday Discussions that was held in Glasgow, Scotland, on advances in supramolecular gels, between the 30th of April and the 2nd of May 2025.

This review provides readers with an updated understanding of supramolecular hydrogels and highlights current research presented during the Faraday Discussions meeting on advances in supramolecular gels.

The co-assembly of amphipathic peptides is explored here and we show the physicochemical properties, the core hydrophobic residues’ side-group size and their packing, affect co-assembly occurrence into self-assembling peptide hydrogels.

We present a covalent-supramolecular composite hydrogelator system where self-assembled networks simultaneously influence tunable energy transport, mechanical reinforcement/dissipation, and processability.

A superficially autocatalytic, self-replicating system is presented that utilises dynamic imine chemistry coupled with self-assembling supramolecular hydrogelation kinetics driven by a nucleation autocatalytic cycle (autoinduction).

Nano-IR sheds light on multicomponent hydrogels to discriminate between self-sorted and co-assembled peptide fibrils.

We combine two bottom-up routes that occur under mild conditions, self-assembly and sol–gel synthesis, to program the shape and structure of materials.

We investigate the relationship between sequence and supramolecular structure for a pair of bola-amphiphilic peptides, Ac-KLIIIK-NH₂ and Ac-KIIILK-NH₂, that self-assemble into supramolecular hydrogels based on cross-b amyloid fibrils.

The presence of BSA induces the hydrogelation of L-peptides but not of their D-enantiomers. Molecular dynamics simulations show that L-peptides interact on the surface of BSA by defolding, thus promoting the interaction of additional L-peptides.

Herein, we study the role that hydrophobicity plays in the temperature-dependent self-assembly of a family of β-hairpin peptide amphiphiles through the lens of thermally folding a protein from its cold-denatured state.

A hydrogel composed of a photoresponsive peptide, agarose, and upconversion nanoparticles responds to NIR light irradiation. The nanoparticles convert NIR light to UV light, triggering a reversible gel-to-sol transition by peptide isomerization.

Cryo-SEM reveals heterogeneous network structure of crosslinked protein-based hydrogels.

Automated descriptors to relate peptide self-assembly with macroscopic properties, enabling machine learning for targeted supramolecular gel discovery.

This study examines how hydrophobic amino acid linkers affect two-component peptide co-assembly. AA linkers promote bilayer sheets, while others favor 1D fibers or fail to aggregate, highlighting hydrophobic linkers’ role in assembly morphology.

Phytantriol and monoolein form lyotropic liquid crystalline gel phases in excess solvent in aqueous ionic liquid and deep eutectic mixtures.

Molecular dynamics simulations provide insights into all stages of supramolecular network formation, from primary nucleation through fiber elongation and secondary nucleation to the assembly of single fibers into bundles.

Supramolecular gelator salt C₁₄·2MAF, derived from hexadecanedioic acid and anti-bacterial drug mafenide, showed anti-bacterial activity against E.coli, serving as a potential vehicle-free drug delivery system.

The study compares the impact of salt form (TFA vs. HCl) on the biostability, cell cytotoxicity, drug release and rheological properties of a Napffky(p)G-OH peptide hydrogel platform that demonstrates promise as a long-acting drug delivery system.

The properties of supramolecular hydrogels of cationic phenylalanine derivatives are modified by multicomponent formulation with anionic amino acids.

Sonani et al. used cryo-EM to determine the atomic structure of CarbIF nanotubes, which helped understand the mechanisms of assembly and gelation.

We have developed a series of rheological and scattering methods to characterise hydrogels 3D printed from low molecular weight gelators, before, during, and after printing.