NBO

Novel Biomimetic Organocatalysts

 Coordinatore THE PROVOST, FELLOWS, FOUNDATION SCHOLARS & THE OTHER MEMBERS OF BOARD OF THE COLLEGE OF THE HOLY & UNDIVIDED TRINITY OF QUEEN ELIZABETH NEAR DUBLIN 

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 Nazionalità Coordinatore Ireland [IE]
 Totale costo 1˙249˙772 €
 EC contributo 1˙249˙772 €
 Programma FP7-IDEAS-ERC
Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call ERC-2007-StG
 Funding Scheme ERC-SG
 Anno di inizio 2008
 Periodo (anno-mese-giorno) 2008-10-01   -   2014-09-30

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    THE PROVOST, FELLOWS, FOUNDATION SCHOLARS & THE OTHER MEMBERS OF BOARD OF THE COLLEGE OF THE HOLY & UNDIVIDED TRINITY OF QUEEN ELIZABETH NEAR DUBLIN

 Organization address address: College Green -
city: DUBLIN
postcode: 2

contact info
Titolo: Ms.
Nome: Deirdre
Cognome: Savage
Email: send email
Telefono: +353 1 8961942
Fax: +353 1 7071633

IE (DUBLIN) hostInstitution 0.00
2    THE PROVOST, FELLOWS, FOUNDATION SCHOLARS & THE OTHER MEMBERS OF BOARD OF THE COLLEGE OF THE HOLY & UNDIVIDED TRINITY OF QUEEN ELIZABETH NEAR DUBLIN

 Organization address address: College Green -
city: DUBLIN
postcode: 2

contact info
Titolo: Prof.
Nome: Stephen
Cognome: Connon
Email: send email
Telefono: 35318961306
Fax: 35316712826

IE (DUBLIN) hostInstitution 0.00

Mappa


 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

active    efficient    cofactor    action    artificial    catalyst    first    enzymes    nad    catalytic    aldehyde    nucleophilic    dehydrogenases   

 Obiettivo del progetto (Objective)

'The primary aim of this project is to substantially expand the frontiers of current benchmark organocatalytic technology by the design, preparation and evaluation of the first class of thiol-based nucleophilic catalyst capable of emulating the action of NAD-dependant enzymes such as aldehyde dehydrogenases, which promote the chemoselective oxidation/reduction of aldehyde substrates under mild conditions in aqueous media. The proposed artificial enzymes are designed biomimetically (in the true sense of the word) – only careful examination of the core enzyme competencies, modes-of-action and active sites has guided the design process. One of the key issues which this proposal addresses is the inherent difficulty associated with the design of artificial cofactor-dependent enzymes due to the requirement for a) efficient recognition by the catalyst of both the substrate and the cofactor, and b) the exertion of control over their encounter in the active site. We intend to tackle this challenge by covalently attaching groups functionally equivalent to the catalytically active residues of aldehyde dehydrogenases to a rigid NAD analogue in a manner which allows for their synergistic and biomimetic cooperation. Structure determination/mechanistic studies and the application of these new catalysts in a range of oxidations/reductions (we envisage that this project will result in the first organocatalyst able to demonstrably promote either - depending on the reaction conditions), (dynamic) kinetic resolutions, desymmetrisations, and ligations) will be undertaken and the development of catalytic processes for reactions currently outside the scope of any catalytic methodology is a clear long-term goal. We also wish to pursue the application of this potentially groundbreaking nucleophilic catalytic technology (for which no efficient organocatalysts have been thus far reported) toward the selective synthesis of enantiopure building blocks and pharmaceutically relevant molecules.'

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