4.7 Article

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

Journal

JOURNAL OF COLLOID AND INTERFACE SCIENCE
Volume 588, Issue -, Pages 580-588

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jcis.2020.12.066

Keywords

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

Funding

  1. Higher Education Commission (HEC) Pakistan
  2. Agence Nationale de la Recherche (EASA) [ANR-18-CE06-0025-03]
  3. Institut Carnot MICA (DIAART)
  4. Agence Nationale de la Recherche (ANR) [ANR-18-CE06-0025] Funding Source: Agence Nationale de la Recherche (ANR)

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The spatial control of supramolecular self-assembly plays a vital role in the design of artificial cells, with the study demonstrating the successful self-assembly of phosphorylated peptides on complex coacervate microdroplets. This process leads to the formation of structured peptide/PAH capsules and fibrillar self-assembled structures at interfaces, showing potential for the development of compartmentalized structures in artificial cells.
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.

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