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

Year: 2021

Journal: J. Colloid Interface Sci., Volume 588, APR 15, page 580–588

Authors: Criado-Gonzalez, Miryam; Wagner, Deborah; Iqbal, Muhammad Haseeb; Ontani, Aymeric; Carvalho, Alain; Schmutz, Marc; Schlenoff, Joseph B.; Schaaf, Pierre; Jierry, Loic; Boulmedais, Fouzia

Organizations: Higher Education Commission (HEC) Pakistan; Agence Nationale de la Recherche (EASA) [ANR-18-CE06-0025-03]; Institut Carnot MICA (DIAART)

Keywords: Coacervates; Polyelectrolytes; Peptides; Supramolecular self-assembly; Layer-by-layer; Multilayers; Fmoc-FF

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. (C) 2020 Elsevier Inc. All rights reserved.