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Structure Function Paradigms in Protein Drug Targets

We build the puzzle of how proteins work for advancing applications in technology and medicine.


Cross-α amyloid-like fibrils secreted by the golden bacterium S. aureus are toxic to human T cells

Tayeb-Fligelman et al. Science 355(6327): 831-833; 2017

Cross-alpha fibrils from S. aureus are toxic to human T cellsImage created by Dima Abelski, Dimedia


Our set of tools:

Integrating X-ray crystallography, electron microscopy, biochemistry, cell biology, bioinformatics and small-molecule design.


Systems of interest:

Developing novel antibiotics is a major public-health priority – The growing numbers of bacteria already fully resistant to every clinical antibiotic available, along with a discovery void of new antibiotics in the last 30 years, puts this field at the front of fundamental and translational research.
We focus on antivirulence activity that may elicit less resistance as the evolutionary pressure on the microbe is less profound compared to bactericidal drugs.
Microbial Functional Amyloids are one of the promising novel targets for antimicrobial agents, since they serve as key virulence factors in many pathogenic bacteria.
Protein involved in Biofilm structuring are our targets for antibiotics against human, animal, and environmental resistance and resilient infections.



Platelet surface receptors – These proteins are essential for maintaining hemostasis and thrombosis, and play key roles in pathophysiological processes related to development, immune responses and cancer. Understanding the mechanisms of action and regulation of these receptors would lay the basis for the development of drugs that will target a range of cardiovascular conditions, bleeding scenarios, cancer, snake envenomation and virus dissemination.


Proteins associated with rare diseases – because we think it is the academia’s role to advance drug discovery for unprofitable conditions.