We are interested in research questions that lie on the interface of chemistry and biology. The research projects that we are involved in are rooted within medicinal chemistry and biological chemistry, and we apply synthetic organic chemistry to address our research questions. Several of our projects require access to synthetic peptides, and the group has established and runs the Peptide synthesis laboratory at the Department of Chemistry. The group has been instrumental for the establishment of the Laboratory for High-throughput experimentation – HTE@UiB.

Professor Haug leads the Norwegian Open Laboratory for High-Throughput Experimentation and Scale-up (NorHTE), which is under establishment as a national infrastructure funded by the Research Council of Norway.

Addressing the need for new antibiotics through under-explored bacterial targets

There is an urgent need for new antibiotics to prevent the looming crisis of antimicrobial resistance. Antibiotics are a prerequisite for modern medicine, and the WHO has published a list of bacteria for which antibiotics are in high demand and urged that research and drug discovery efforts are directed toward these. To tackle this crisis, we need fundamental knowledge on new targets for antibiotics, and we need compounds that can get into bacteria and work on these targets.

In our work, we are contributing to addressing the global AMR crisis through design and synthesis of riboswitch ligands and inhibitors of bacterial fatty acid synthesis.

The group is part of the TargetRNA Marie Skłodowska-Curie Action (MSCA) doctoral training network and the LEAD AI research and training program for future AI leaders funded by the MSCA COFUND-scheme.

Molecular imaging

We are working on developing new methods for radiolabeling of peptides and peptide-based probes for PET-imaging and are part of the Tracer Development Center of the Norwegian Nuclear Medicine Consortium. We are also working on the development of new probes for optical imaging and new applications for these.

Inhibitors of N-terminal acetyl transferases

Proteins constitute an essential part of the machinery of life and display enormous variation in both structure and function. In addition to the diversity inferred by the 20 coded amino acids, proteins are often covalently modified during or after biosynthesis, which adds additional layers of complexity.

Acetylation is one of the most common co- or post-translational protein modifications, and occurs either on the amino group of lysine side chains (K-acetylation) or on the alpha-amino group of N-terminal residues (Nt-acetylation).

Nt-acetylation of proteins is extremely common and occurs on more than 80% of all human proteins. Biochemically it consists of transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the protein substrate and is catalysed by the N-terminal acetyltransferase (NAT) group of enzymes.

Although our understanding of the NATs has increased in recent years, there are fundamental questions that remain unanswered in the field:
– What are the cellular roles of NAT enzymes (and thus Nt-acetylation)?
– Can NATs be targeted for therapeutic intervention in cancer and other diseases?

Access to specific and potent NAT inhibitors is a prerequisite to answer these questions, and we are working toward equipping the scientific community with these molecular tools.