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PROFOLIG SIGNED

Covalent-ligation-assisted elucidation of protein-aromatic foldamer interactions

Total Cost €

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EC-Contrib. €

0

Partnership

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 PROFOLIG project word cloud

Explore the words cloud of the PROFOLIG project. It provides you a very rough idea of what is the project "PROFOLIG" about.

directed    explore    consists    disulfide    tunable    purpose    helix    appear    validate    essentially    expressed    proteinogenic    kda    bind    first    tether    assistance    display    therapy    secondary    interleukin    mimetics    aromatic    recognition    molecule    induction    amides    molecular    intend    chiral    combining    initiate    pool    iterative    solution    area    bearing    ribosome    mainly    relatively    screening    pharmacology    conformations    of    synthetic    amenability    handedness    helical    structure    synthesis    cystein    15    medium    tertiary    stable    rules    predictable    bridge    adducts    oligoamide    recombinantly    optimized    epitope    sequences    crystallography    evolution    strategy    principles    ligands    selectively    unexplored    small    structures    backbones    ultimately    diagnostics    surface    alpha    chains    structural    foldamer    interactions    il4    proteins    foldamers    characterization    mutant    crystal    thanks    sized    suited    attachment    protein    elucidation    covalent   

Project "PROFOLIG" data sheet

The following table provides information about the project.

Coordinator
CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE CNRS 

Organization address
address: RUE MICHEL ANGE 3
city: PARIS
postcode: 75794
website: www.cnrs.fr

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country France [FR]
 Project website http://www.iecb.u-bordeaux.fr/teams/BISE/
 Total cost 185˙076 €
 EC max contribution 185˙076 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2016
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2017
 Duration (year-month-day) from 2017-03-01   to  2019-02-28

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE CNRS FR (PARIS) coordinator 185˙076.00

Map

 Project objective

The development of ligands that selectively bind to a given protein surface is a challenging area of research with potential applications in diagnostics, pharmacology or therapy. Current approaches include small molecule screening, the design of medium sized epitope mimetics (e.g. alpha helix mimetics) and directed evolution methodologies (e.g. ribosome display).

In this project, we intend to initiate an essentially unexplored approach: the design from first principles of synthetic ligands derived from helical aromatic oligoamide foldamer backbones bearing proteinogenic side chains to target the surface of a given protein: interleukin 4 (IL4). Helical aromatic amides appear to be well suited for this purpose thanks to their predictable, tunable and stable conformations in solution; their relatively easy synthesis of secondary and tertiary-like structures as large as small proteins; and their high amenability to crystal growth and structural elucidation. Specifically, we intend to explore molecular recognition rules between large (2-15 kDa) aromatic oligoamide foldamers and a target protein surface, and to validate a novel iterative method based on combining covalent attachment and structural characterization.

The proposed strategy thus consists in structure-based iterative design. The following steps will be implemented: 1) synthesis of a small pool of foldamer sequences; 2) covalent attachment of each of them via a disulfide bridge to the surface of a recombinantly expressed IL4 cystein mutant, and screening for foldamer-protein interactions through foldamer helix handedness induction by the chiral protein surface; 3) structural characterization of the interactions, mainly by crystallography, within selected protein-foldamer adducts; 4) design of new and improved foldamers. Ultimately optimized interactions should produce foldamers that bind to IL4 without the assistance of the covalent tether.

 Publications

year authors and title journal last update
List of publications.
2018 Maëlle Vallade, Post Sai Reddy, Lucile Fischer, Ivan Huc
Enhancing Aromatic Foldamer Helix Dynamics to Probe Interactions with Protein Surfaces
published pages: 5489-5498, ISSN: 1434-193X, DOI: 10.1002/ejoc.201800855
European Journal of Organic Chemistry 2018/40 2019-05-27

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