Research

Proteins are nature’s most powerful machineries, responsible for essential biological functions, including catalysis, signal transduction, molecular recognition, and many more. As such, they are involved in almost all fundamental processes. What has always inspired and fascinated chemists and biochemists is the complex and intricate relationship between their structure and function leading to unique chemo-, regio- and stereoselectivities in biological reactions, carried out under mild conditions. The question we explore in our group is whether the vast conformational space of oligopeptides and proteins is amenable to ab initio structural predictions.

Among various essential elements in biocatalysis, metalloproteins play a specific role by catalyzing reactions that would not occur under physiological conditions. The presence of metal ions is crucial for the oxidation/reduction processes, electron transfer, spin-forbidden reactions and ‘difficult reactions’, such as N₂, O₂, C–H bond cleavage (or formation). These processes are intimately involved in the fundamental processes of life, e.g. respiration and photosynthesis. 

Short peptides that bind toxic metals, such as lead, or overabundant metals during diseases, can provide therapeutic agents for metal poisoning.

Understanding catalytic properties of metal centers and the ability to emulate them in green biochemical catalysts could prove invaluable to various fields of science and industry.

Quantum mechanics is finding its way into computational ligand design. We expect it to replace force field approaches whose accuracy is limited. In our group, we participated in two multidisciplinary projects within the Gilead Sciences Research Center in Prague (GSRCP-3, and GSRCP-4). Two systems (proteins) of interest were STING (stimulator of interferon genes) and human rhinovirus protease 3C (HRV 3C).

We have provided evidence of the decades old proposal of existence of Au(I)···H hydrogen bonds. Inspired by the existence of Au(I)···H interaction, we pursue - experimentally and theoretically - the Ag(I)···H hydrogen bond.  

In collaboration with Dr. Mirco Natali (University of Ferrara) and Dr. Albert Ruggi (University of Fribourg) we combine state-of-the-art computations with electrochemistry and photochemistry to explore the potential of newly synthesized iron and cobalt complexes for CO₂ reduction reaction (CO₂RR).

One of the alternatives for how to make computers faster and smaller is molecular electronics that pursues the idea of single molecules acting as electronic components. Independently, molecules can also act as molecular switches and motors. We try to fuse these two fields by designing switching molecular electronics.

The interior of a fullerene cage is an excellent “nanolab” that enables clusters and bonding unseen elsewhere, for example actinide-actinide bonds.

Together with experimentalists we study metal complexes that are meant to be applied in radiotherapy and diagnostics. Our most recent contribution brings ultra-inert lanthanide-chelates with kinetic inertness up to a million-fold relative to lanthanide DOTA complexes, expanding utility of lanthanide chelates beyond traditional uses.

We have provided a unified understanding and rules how heavy-atoms across the periodic table affekt NMR chemical shifts of their neighbouring atoms. Simple rules introduced help to  experiment with understanding exotic NMR signals found at unexpected chemical shift ranges, e.g. in Pb(II) compounds.