SAMUL-NANO-HEP

Self-Assembling Multivalent Biodegradable Ligands for Nanoscale Heparin Binding

Coordinatore	UNIVERSITY OF YORK    more  Organization address address: HESLINGTON city: YORK NORTH YORKSHIRE postcode: YO10 5DD contact info Titolo: Mr. Nome: Chris Cognome: Barber Email: send email Telefono: +44 1904 324416
Nazionalità Coordinatore	United Kingdom [UK]
Totale costo	221˙606 €
EC contributo	221˙606 €
Programma	FP7-PEOPLE Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	FP7-PEOPLE-2013-IEF
Funding Scheme	MC-IEF
Anno di inizio	2014
Periodo (anno-mese-giorno)	2014-10-01   -   2016-09-30

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	UNIVERSITY OF YORK  Organization address address: HESLINGTON city: YORK NORTH YORKSHIRE postcode: YO10 5DD contact info Titolo: Mr. Nome: Chris Cognome: Barber Email: send email Telefono: +44 1904 324416	UK (YORK NORTH YORKSHIRE)	coordinator	221˙606.40

Mappa

 Word cloud

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

 Obiettivo del progetto (Objective)

'This proposal targets the development of self-assembling nanoscale systems to bind heparin. Heparin is widely used as an anti-coagulant during major surgery, but once surgery is complete, it is necessary to remove the heparin and allow clotting to begin. The current therapy is protamine, a protein extracted from shellfish which acts as a powerful heparin binder, but unfortunately, causes allergic response and other problems in significant numbers of patients (ca. 10%). We are therefore targeting the development of novel synthetic nanoscale protamine replacements which may avoid some of these difficulties. Our unique strategy is to develop small molecules which self-assemble into nanoscale heparin binders. This has the advantage of being highly tunable and uses low molecular-weight (drug-like) building blocks – allowing structure-activity relationship understanding of the binding event to emerge. The self-assembled structures will be optimised in terms of their charge density, morphology, display of functional groups and ability to degrade, to maximise heparin binding and surgical potential. This project will provide fundamental insight into the requirements of an effective heparin binder. Our optimised systems will be tested in clotting and toxicity assays, and may have longer-term applications in a medical setting.'