SAMUL-NANO-HEP

Self-Assembling Multivalent Biodegradable Ligands for Nanoscale Heparin Binding

 Coordinatore 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

 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

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clotting    nanoscale    protamine    surgery    binding    self    binder    heparin   

 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.'

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