CE06 - Polymères, composites, physique et chimie de la matière molle

Peptide- Polymerization Induced Self-Assembly – PEPPISA

Submission summary

Since its inception in 2010, Polymerization-Induced Self-Assembly (PISA) has revolutionized the way polymer scientists synthesize block copolymers self-assembled nano-objects. PISA consists in synthesizing a solvophobic polymer block from a solvophilic polymer block usually using controlled radical polymerization techniques in dispersed media such as RAFT dispersion (or emulsion) polymerization. As the solvophobic polymer block grows, the in-situ formed amphiphilic block copolymer self-assembles to minimize the solvent-polymer interactions. PISA is very advantageous compared to other polymer self-assembly techniques since it allows the preparation of a variety of polymer morphologies (such as spherical micelles, worm-like micelles which often form physical gels, vesicles or framboidal particles to name a few) with a very high degree of purity (mixed morphologies often observed with other self-assembly techniques can be avoided), a very high degree of reproducibility, and in high concentrations (up to 50 % solids content).
Peptides and proteins are a pivotal class of biological or synthetic oligomers that possess an almost endless variety of structural and functional properties. They constitute the core of the biological machinery and are involved in virtually all living organism processes. Proteins and peptides secondary, tertiary, and quaternary structures are generally governed by non-covalent interactions such as hydrogen bonds, metal ion chelation, p-p stacking, van der Waals forces and so on. Relying on these interactions, simpler synthetic peptide structures able to self-assemble (self-assembling peptides (SAP)) were designed to provide supramolecular assemblies. SAP form organized tridimensional architectures such as fibers, ribbons, nano-tubes or nano-particles by interacting with each other via specific non-covalent interactions.
The combination of the self-assembling properties of SAP and the PISA process to get hybrid organized polymer-peptide structures has never been explored. The mechanism at work in the self-assembly of diblock copolymer structures (worm-like structures, spheres, vesicles …) obtained by PISA relies almost only on hydrophilic-lipophilic balance, just like the majority of block-copolymer self-assembly work. Some studies have shown that electrostatic interactions, in the case of purely polycationic and polyanionic hydrophilic stabilizers, were detrimental to the formation of higher order morphologies and restricted the PISA particles to spherical shapes.
In this context, PEPPISA proposes to investigate the original combination of PISA with SAP as inducers of structuration during or after the polymerization process. More precisely, we will study the effect of peptides specific interactions on the morphologies of objects obtained by PISA. We aim to answer the following scientific questions:
- How do SAP influence the PISA self-assembly process?
- What is the influence of the location of the SAP in the nano-objects?
- Can these SAP-containing particles form higher order supramolecular constructs?
PEPPISA will thus examine the interplay of the kinetically-governed self-assembly of diblock copolymers using PISA protocols and the likely thermodynamically-controlled structuring effect of peptide sequences. This pioneering project will provide a better understanding of the complex competitive or synergetic mechanisms at work during the self-assembly of peptide diblock copolymers.

Project coordination

Mona SEMSARILAR (Institut Européen des Membranes)

The author of this summary is the project coordinator, who is responsible for the content of this summary. The ANR declines any responsibility as for its contents.


IEM Institut Européen des Membranes

Help of the ANR 195,404 euros
Beginning and duration of the scientific project: October 2019 - 42 Months

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