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Our research focuses on developing protein modulators in order to study structure-function aspects of cellular protein networks and to develop new drugs targeting protein-protein interactions (PPIs) with both small molecules and optimized protein variants. Drug discovery is a multidisciplinary science by nature and requires the understanding and application of biology, chemistry, pharmacology and biophysical tools.

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Small molecules

Small molecules are chemical entities with the size of about 500 Da and with additional drug-like chemical and physical properties. These type of molecules is an important part in the arsenal of therapeutics. The discovery of small molecules targeting PPIs is a challenging scientific path. Unlike enzymes, PPIs have a large and shallow interface and do not result in an outcome assay.

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Among the different approached for the discovery of small molecules targeting specific protein, the integration of computational and biophysical tools is a promising path to the discovery of PPI inhibitors.

 

 

Peptides/protein design

A different approach to modulate protein-protein interactions is to rely on nature itself. For that purpose, one of the partner proteins or a fragment (peptide) of it can be further optimized using lab-evolution tools. These entities are much larger than the former small molecules where peptides range 1-5 kDa and protein are usually larger than 10 kDa.

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Some optimized proteins interfering with PPIs show better activity profile than antibodies and thus pose a promising therapeutic path.

 

 

 

 

Current projects in the lab are dealing with:

  1. Discovery of small molecules targeting new Protein-Protein interactions

  2. Design of anti-inflammation and anti-fungal optimized peptides for wide range of applications.

  3. New immune-suppression solutions targeting the calineurin-NFAT interaction

  4. Developing an optimized proteins as Triple-Negative Breast Cancer markers for MRI applications

  5. Optimized proteins as a novel non-antibody biologic immunotherapy drug

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