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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.

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

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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