This research group is led by Seino Jongkees and Ivana Drienovska.
Group Seino Jongkees
The Jongkees group (Chemical Biology and Biotechnology) uses chemical and biological tools to conduct research at the interface of peptides, proteins, nucleic acids and carbohydrates.
Research in our group focuses on genetic code reprogramming, bio-orthogonal chemistry and high throughput in vitro peptide display. Using these advanced chemical and biochemical technologies, we aim to define a new class of ligands for investigating and modulating proteins, particularly proteins involved in carbohydrate biology. These small de novo macrocyclic peptides decorated with non-canonical functional groups have exemplary affinity and selectivity and are applicable to a wide variety of targets. Research in the group is focused on the development of new methods for library modification, including novel non-canonical amino acids for incorporation by ribosomal translation and novel chemo-selective reactions for modification after translation, as well as the application of these technologies to discover new chemical entities for biological studies and drug development. Our research includes synthetic organic chemistry of both building blocks and peptides, analytical studies of novel reactions, optimization of in vitro translation conditions, biochemical characterization of interactions with proteins and in vitro selection to discover new bioactive molecules.
Group Ivana Drienovská
The group aims to deliver versatile biocatalytic platforms with relevance for drug synthesis, sustainable chemical transformations, and chemical biology.
Research in the Drienovská Group focuses on expanding the catalytic potential of enzymes beyond what is accessible in nature. We combine genetic code expansion, protein engineering, and mechanistic enzymology to create new-to-nature biocatalysts with tailored reactivity, selectivity, and function. By incorporating non-canonical amino acids into proteins, we introduce novel chemical functionalities into enzyme active sites, enabling catalytic strategies unavailable to the natural amino acid repertoire. These approaches allow the design of artificial and hybrid catalytic systems, including organocatalytic and photocatalytic enzymes, in which non-natural functionalities are directly integrated into the protein scaffold. In parallel, we investigate fundamental questions at the interface of chemistry and biology, including how new catalytic functions emerge, how enzyme mechanisms can be reprogrammed, and how protein environments can be engineered to operate under non-natural reaction conditions.
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