Bengt Erik Haug

Stilling

Professor

Tilhørighet

Forskergrupper

Forskning

Vi er interessert i forskningsspørsmål som ligger på grensesnittet mellom kjemi og biologi. Forskningsprosjektene vi er involvert i er forankret i legemiddelkjemi og biologisk kjemi, og vi bruker syntetisk organisk kjemi som metode for å addressere våre forskningsspørsmål. Gruppen har hatt en viktig rolle i etableringen av Laboratory for high-throughput experimentation - HTE@UiB, som professor Haug leder. Flere av prosjektene vi jobber med krever også tilgang til syntetiske peptider, og gruppen har etablert og driver Laboratorium for peptidsyntese ved Kjemisk institutt.

Gruppen er del av forskningsgruppen for Bioressurser og farmasøytisk kjemi.

Publikasjoner
Kronikk
Vitenskapelig artikkel
Vitenskapelig foredrag
Poster
Doktorgradsavhandling
Populærvitenskapelig foredrag
Vitenskapelig oversiktsartikkel/review
Faglig foredrag
Sammendrag/abstract
Kompendium
Annet produkt
Populærvitenskapelig artikkel

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Prosjekter

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.

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.