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HiChemSynPro SIGNED

High-throughput combinatorial chemical protein synthesis as a novel research technology platform for chemical and synthetic biology

Total Cost €

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EC-Contrib. €

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Partnership

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Project "HiChemSynPro" data sheet

The following table provides information about the project.

Coordinator
CENTRE INTERNATIONAL DE RECHERCHE AUX FRONTIERES DE LA CHIMIE FONDATION 

Organization address
address: ALLEE G MONGE 8
city: STRASBOURG
postcode: 67000
website: http://www.icfrc.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]
 Total cost 1˙500˙000 €
 EC max contribution 1˙500˙000 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2016-STG
 Funding Scheme ERC-STG
 Starting year 2017
 Duration (year-month-day) from 2017-03-01   to  2022-02-28

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    CENTRE INTERNATIONAL DE RECHERCHE AUX FRONTIERES DE LA CHIMIE FONDATION FR (STRASBOURG) coordinator 1˙500˙000.00

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 Project objective

Chemical protein synthesis is an indispensable method in chemical and synthetic biology. However, at the present moment, it is laborious and involves multiple optimization and purification steps. High-throughput approaches for total synthesis of combinatorial libraries of custom-modified protein variants are needed. To change the situation, the work will be carried out in two directions: (1) implementation of microfluidic techniques for automation, miniaturization and multiplexing of experimental steps involved in the total synthesis of proteins, and (2) design and synthesis of novel catalytic proteins for efficient enzyme-assisted peptide ligations under denatured conditions. This innovative research technology will allow robust chemical synthesis of protein libraries with (100–10,000)-compounds with natural and unnatural modifications, bearing variety of post-translational modifications and also protein-like biopolymers. In this project, the new methodology will be validated by chemical synthesis of library of phosphorylated analogues of high mobility group protein A (HMGA), which is involved in gene-transcription and cancer development. Other potential future applications include protein design, biological problems where post-translational modifications play a crucial role (ranging from the ‘histone code’ hypothesis to understanding long-term memory) and functional annotation of newly discovered genes.

 Publications

year authors and title journal last update
List of publications.
2018 Régis Boehringer, Bruno Kieffer, Vladimir Torbeev
Total chemical synthesis and biophysical properties of a designed soluble 24 kDa amyloid analogue
published pages: 5594-5599, ISSN: 2041-6520, DOI: 10.1039/c8sc01790e
Chemical Science 9/25 2019-10-29
2019 Abhishek Baral, Aromal Asokan, Valentin Bauer, Bruno Kieffer, Vladimir Torbeev
Chemical synthesis of transactivation domain (TAD) of tumor suppressor protein p53 by native chemical ligation of three peptide segments
published pages: 703-708, ISSN: 0040-4020, DOI: 10.1016/j.tet.2018.11.074
Tetrahedron 75/6 2019-10-29

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