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DENOPHECK SIGNED

Purposing de novo protein scaffolds for the Heck reaction

Total Cost €

0

EC-Contrib. €

0

Partnership

0

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 DENOPHECK project word cloud

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

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Project "DENOPHECK" data sheet

The following table provides information about the project.

Coordinator
UNIVERSITAT BAYREUTH 

Organization address
address: UNIVERSITATSSTRASSE 30
city: BAYREUTH
postcode: 95447
website: www.uni-bayreuth.de

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 Germany [DE]
 Total cost 162˙806 €
 EC max contribution 162˙806 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2019
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2020
 Duration (year-month-day) from 2020-09-01   to  2022-08-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    UNIVERSITAT BAYREUTH DE (BAYREUTH) coordinator 162˙806.00

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 Project objective

The overall aim of this fellowship is to develop an enzymes that catalyses the Heck reaction using de novo proteins.

We now live in an age where the consequences of the emissions of greenhouse gases are having observable, detrimental effects on our planet’s ecosystem. Therefore, the need to develop non-toxic, cleaner and lower energy reactions is essential. Palladium(0)-catalysed cross-coupling reactions are a powerful method for generating carbon-carbon and carbon-heteroatom bonds, leading to their extensive use in academia and industry. Among all cross-coupling reactions, it can be argued that the Heck reaction is one of the greenest because the reagents are not prefunctionalised with metals, boron or silicon. Furthermore, it has been demonstrated that the Heck reaction can be performed in water, although truly catalytic examples to date require temperatures up to 140 °C and often more reactive and expensive aryl bromide and aryl iodide reagents.

De novo protein design, the selection of an amino-acid sequence that will fold to a desired protein structure, is a newly established field. Successful designs have furnished a diverse range of protein structures. In contrast to most natural proteins, de novo proteins are well understood, have high thermal stability and are characterised to atomic detail.

Dr Rhys, under the supervision of Prof Höcker & Prof Weber, proposes to purpose a range of de novo proteins to bind artificial co-factors to develop truly de novo Heckase enzymes. Functional enzymes will be optimised using well-established rational design and directed-evolution techniques.

The development of an optimised Heckase could overcome existing challenges to produce an ambient temperature, stereoselective, water-soluble Heck catalyst.

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The information about "DENOPHECK" are provided by the European Opendata Portal: CORDIS opendata.

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