Bengt Erik Haug

Position

Professor

Affiliation

Research groups

Research

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. The group has been instrumental for the establishment of the Laboratory for High-throughput experimentation - HTE@UiB, which is lead by Professor Haug. 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 is part of the research group on Bioresources and Pharmaceutical Chemistry.

Publications
Feature article
Academic article
Academic lecture
Poster
Doctoral dissertation
Popular scientific lecture
Academic literature review
Lecture
Abstract
Compendium
Popular scientific article
Other product

See a complete overview of publications in Cristin.

Projects

Addressing the need for new antibiotics through underexplored bacterial targets

The group in involved in several research projects where novel targets for future antibiotics are investigated. Our focus is on processes that are essential in bacteria and in our work, we address several different riboswitches, which are non-coding structural elements in mRNA that regulate gene expression by binding to small organic molecules, in addition to key enzymes within the fatty acid synthesis machinery in bacteria.

The group is a partner in the EU Horizon funded Marie Skłodowska-Curie Action (MSCA) doctoral training network TargetRNA.

Early drug discovery

The group is partner in the RESPOND3 project on responsible early digital drug discovery within the Centre for Digital Life Norway. This project focuses on developing better computational approaches and responsible innovation strategies in early drug discovery with applications to antibiotics targeting riboswitches and inflammatory lung diseases.

Molecular imaging

The group is part of the Tracer Development Center of the Norwegian Nuclear Medicine Consortium.

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 catalyzed 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 in collaboration with the Arnesen group at UiB.