Localized Enzyme-Assisted Self-Assembly of low molecular weight hydrogelators. Mechanism, applications and perspectives.

Nature uses systems of high complexity coordinated by the precise spatial and temporal control of associated processes, working from the molecular to the macroscopic scale. This living organization is mainly ensured by enzymatic actions. Herein, we review the concept of Localized Enzyme-Assisted Self-Assembly (LEASA). It is defined and presented as a straightforward and insightful strategy to achieve high levels of control in artificial systems. Indeed, the use of immobilized enzymes to drive self-assembly events leads not only to the local formation of supramolecular structures but also to tune their kinetics and their morphologies. The possibility to design tailored complex systems taking advantage of self-assembled networks through their inherent and emergent properties offers new perspectives for the design of novel, more adaptable materials. As a result, some applications have already been developed and are gathered in this review. Finally, challenges and perspectives of LEASA are introduced and discussed.

Supramolecular tripeptide self-assembly initiated at the surface of coacervates by polyelectrolyte exchange.

Spatial control of supramolecular self-assembly can yield compartmentalized structures, a key feature for the design of artificial cells. Inducing self-assembly from and on compartments is still a challenge. Polyelectrolyte complex coacervates are simple model droplet systems able to reproduce the basic features of membrane-less organelles, appearing in cells. Here, we demonstrate the supramolecular self-assembly of a phosphorylated tripeptide, Fmoc-FFpY (Fmoc: fluorenyl-methoxycarbonyl; F: phenyl alanine, pY: phosphorylated tyrosine), on the surface of poly(l-glutamic acid)/poly(allylamine hydrochloride) (PGA/PAH) complex coacervate microdroplets. The phosphorylated peptides self-assemble, without dephosphorylation, through ion pairing between the phosphate groups of Fmoc-FFpY and the amine groups of PAH. This process provides spontaneous capsules formed by an amorphous polyelectrolyte complex core surrounded by a structured peptide/PAH shell. Similar fibrillar Fmoc-FFpY self-assembled structures are obtained at the interface between the peptide solution and a PGA/PAH polyelectrolyte multilayer, a complex coacervate in the thin film or "multilayer" format. In contact with the peptide solution, PAH chains diffuse out of the coacervate or multilayer film and complex with Fmoc-FFpY at the solution interface, exchanging any PGA with which they were associated. Self-assembly of Fmoc-FFpY, now concentrated by complexation with PAH, follows quickly.