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

Fiche publication

Date publication

janvier 2021

Journal

Journal of colloid and interface science

Auteurs

Membres identifiés du Cancéropôle Est :
Pr SCHAAF Pierre , Dr SCHMUTZ Marc

Tous les auteurs :
Criado-Gonzalez M, Wagner D, Iqbal MH, Ontani A, Carvalho A, Schmutz M, Schlenoff JB, Schaaf P, Jierry L, Boulmedais F

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/33450601

Résumé

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.