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3D BIOMIMETICS

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Scaffold Based Supramolecular Architectures as Protein Epitope Mimetics for Biom...

Scaffold Based Supramolecular Architectures as Protein Epitope Mimetics for Biomedical Applications 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 po... ver más

31/08/2016

UNIMIB

218K€

Presupuesto del proyecto: 218K€

Líder del proyecto

UNIVERSITA DEGLI STUDI DI MILANOBICOCCA No se ha especificado una descripción o un objeto social para esta compañía.

TRL 4-5

Fecha límite participación Sin fecha límite de participación.

Financiación concedida El organismo FP7 notifico la concesión del proyecto el día 2016-08-31 No tenemos la información de la convocatoria

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Información adicional privada

No hay información privada compartida para este proyecto. Habla con el coordinador.

1 Participantes

UNIMIB

0.00€ | Lider

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Líder del proyecto

UNIVERSITA DEGLI STUDI DI MILANOBICOCCA No se ha especificado una descripción o un objeto social para esta compañía.

TRL 4-5

Presupuesto del proyecto 218K€

Fecha límite de participación Sin fecha límite de participación.

Descripción del proyecto 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.

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