NCB-TNT

New chemical biology for tailoring novel therapeutics

Coordinatore	THE UNIVERSITY COURT OF THE UNIVERSITY OF ST ANDREWS    more Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie.
Nazionalità Coordinatore	United Kingdom [UK]
Totale costo	2˙499˙991 €
EC contributo	2˙499˙991 €
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-2013-ADG
Funding Scheme	ERC-AG
Anno di inizio	2014
Periodo (anno-mese-giorno)	2014-03-01   -   2019-02-28

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	THE UNIVERSITY COURT OF THE UNIVERSITY OF ABERDEEN  Organization address address: KING'S COLLEGE REGENT WALK city: ABERDEEN postcode: AB24 3FX contact info Titolo: Ms. Nome: Crystal Cognome: Anderson Email: send email Telefono: +44 1224 274103 Fax: +44 1224 272319	UK (ABERDEEN)	beneficiary	525˙761.00
2	THE UNIVERSITY COURT OF THE UNIVERSITY OF ST ANDREWS  Organization address address: NORTH STREET 66 COLLEGE GATE city: ST ANDREWS FIFE postcode: KY16 9AJ contact info Titolo: Ms. Nome: Trish Cognome: Starrs Email: send email Telefono: +44 1334 467286 Fax: +44 1334 442217	UK (ST ANDREWS FIFE)	hostInstitution	1˙974˙230.00
3	THE UNIVERSITY COURT OF THE UNIVERSITY OF ST ANDREWS  Organization address address: NORTH STREET 66 COLLEGE GATE city: ST ANDREWS FIFE postcode: KY16 9AJ contact info Titolo: Prof. Nome: James Henderson Cognome: Naismith Email: send email Telefono: +44 1334 463792 Fax: +44 1334 462217	UK (ST ANDREWS FIFE)	hostInstitution	1˙974˙230.00

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 Obiettivo del progetto (Objective)

'Most of our drugs derive from natural products, many more natural products possess biological activity but our inability to synthesise novel analogues hampers our ability to use them either as tools or medicines. Cyclic peptides are common structural motifs in natural products and medicines (vancomycin, gramicidin). They are widely recognised to constitute a promising and still underexploited class of molecule for novel therapeutics; specifically an important role for cyclic peptides in the inhibition of protein-protein interactions has been demonstrated. We will harness the power of the recently identified macrocyclases from the ribosomally-derived cyanobactin superfamily to prepare diverse modified cyclic peptides. These enzymes exhibit the remarkable ability to macrocyclise unactivated peptide substrates. Different members of this family of macrocyclases process peptides into macrocycles containing from six up to twenty residues. We have characterised and re-engineered one member of the family (PatG) which makes eight residue macrocycles. We will determine the structural and biochemical features of the macrocyclases that are known to lead to six or to twenty residue macrocycles. We will use these insights to put these enzymes to work in novel chemical reactions. We will combine macrocyclases with other enzymes from the cyanobactin biosynthetic pathways (whose structures and mechanism we have largely determined) and work on solid phase peptide substrates. By bringing together the power of solid phase methods (split and pool) and the novel chemistry enabled by the enzymes, we will generate highly diverse macrocyclic scaffolds containing amino acids, enzymatically modified amino acids, non-natural amino acids and non-amino acid building blocks. Successful completion of the project will revolutionise the design of cyclic peptide-inspired libraries with diverse backbone scaffolds for applications in target identification, drug discovery and tool screening.'