3D BIOMIMETICS

Scaffold Based Supramolecular Architectures as Protein Epitope Mimetics for Biomedical Applications

Coordinatore	UNIVERSITA' DEGLI STUDI DI MILANO-BICOCCA    more  Organization address address: PIAZZA DELL'ATENEO NUOVO 1 city: MILANO postcode: IT-20126 contact info Titolo: Dr. Nome: Anastasia Cognome: Sguera Email: send email Telefono: 39264483573
Nazionalità Coordinatore	Italy [IT]
Totale costo	218˙349 €
EC contributo	218˙349 €
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-IOF
Funding Scheme	MC-IOF
Anno di inizio	2014
Periodo (anno-mese-giorno)	2014-03-01   -   2016-08-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	UNIVERSITA' DEGLI STUDI DI MILANO-BICOCCA  Organization address address: PIAZZA DELL'ATENEO NUOVO 1 city: MILANO postcode: IT-20126 contact info Titolo: Dr. Nome: Anastasia Cognome: Sguera Email: send email Telefono: 39264483573	IT (MILANO)	coordinator	218˙349.30

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 Obiettivo del progetto (Objective)

'Synthetic molecules that mimic the structure of the part of a folded protein involved in recognition events (protein epitope mimetics, PEMs) can access biological targets previously deemed as “undruggable” and are considered as a potential source of future therapeutics. So far, PEMs could effectively mimic only individual secondary structure elements of peptides and proteins. The major goal of this project is the development of a novel versatile platform for the design of multifaceted 3D architectures as PEMs of higher order structure elements and discontinuous epitopes of bioactive protein surfaces. The platform is based on cyclic pseudopeptide scaffolds comprising triazole rings linked by conventional amide bonds that are designed to allow for precise topological positioning of biomolecules. The synthetic strategy relies on sequential assembly on solid support of tailor-made building blocks through cycles of alternated amide coupling and Copper(I)-catalyzed azide-alkyne cycloaddition reactions. The building blocks will be prepared in solution and using solid phase synthesis (SPS) to produce macromolecular units bearing bioactive peptide segments. Conclusively, these PEM systems can provide further insight into protein folding mechanism and recognition processes of bioactive protein surfaces. On the other side, improving pharmacodynamic and pharmacokinetic properties of natural peptides and proteins, a number of biomedical applications can be targeted. Specific focus will be devoted to the development of PEM anti-infective agents and the mimicry of structural and functional properties of trimeric HR1 complex of the HIV-1 protein gp41. Moreover, the developed platform can allow for the design of chimeric PEM systems that present saccharide and peptide units in a convergent manner as in the surface of native glycoproteins. This “discontinuous epitope” approach will be applied to improve pharmacological properties of the antimicrobial PEM systems.'