Research

COOPERATE – Engineering of cooperative peptidases

In this project we aim to engineer oligomeric cooperative variants of papain-like cysteine proteases using a combination of rational computer-aided design and experimental screening of mutant protein libraries. The project is sponsored by ARIS (grant no. N1-0211).

Oligomeric states and evolution of DPPI

In close connection with project COOPERATE, we aim to determine the diversity of oligomeric states and dynamics of oligomeric transitions incathepsins C from humans and other eukaryotes.

PRISM – PRotein Interactions with Small Molecules

The acronym PRISM stands for a long-term goal of our group to identify novel bioactive compounds synthesized at UL FKKT. The major emphasis is on identifying compounds with antimicrobial activity and their molecular (protein) targets.

Allosteric regulation of papain-like peptidases

Our major research topic for over a decade that originates from my postdoctoral stay in the lab of prof. Antonio Baici at Uni Zurich. We characterized glycosaminoglycans as the first known allosteric effectors of these peptidases and identified first small molecule allosteric effectors. We also investigated the structural basis for transmission of allosteric communication.

NEWS

Review paper on the diversity of peptidase regulation published in IJMS. Read the full text here.

Review paper on Cathepsin C/DPPI published in Rare Disease and Orphan Drugs Journal. Read the full text here.

Joint effort of MSc students and our collaborators from the Chair of Inorganic Chemistry resulted in a publication in IJMS. Full text here.

Evolutionary history of cathepsin C/ DPPI investigated in our recent publication. Find the full text here.