Specialer

Kasper Dyrberg Rand
Associate Professor
Email: kdr(at)farma.ku.dk 
Telephone: 35336275
Room: 13 – 615 

Structural analysis of biopharmaceuticals by mass spectrometry
Biopharmaceuticals (i.e. protein-based drugs) account for a rapidly growing number of new drugs in development in the pharmaceutical industry. New techniques are needed to characterize these large and complex biomolecules. Mass spectrometry (MS) is uniquely suited to analyze biopharmaceuticals and we have recently developed a range of advanced MS-based methods to analyze the structure, folding, stability of proteins relevant to human disease. In this project you will apply such new MS methods to analyze the structure of a key proteins under different experimental conditions including actual protein drugs of interest at Novo Nordisk (GLP-1 and Insulin). Project work will be done in collaboration with Dr. Kim Haselmann at Novo Nordisk A/S.
Supervisor: Kasper D. Rand.
No of students: 1-2

Studying the binding of small molecule drugs to protein receptors by mass spectrometry
The vast majority of drugs in use to treat human disease targets protein biomacromolecules within the body. The analysis of interactions between ligands and proteins is thus at the core of pharmaceutical research. We have recently developed a method whereby the binding of small molecule ligands to naturally occurring protein receptors can be studied in great structural detail. By using mass spectrometry, we measure the hydrogen/deuterium exchange (HX) of the protein receptor in the absence and presence of a single or a panel of small molecule ligands (HX-MS). We can thus map the binding site of ligands on the protein receptor and study the structural effects of binding. In this project, you will use this method to study the binding of potential small molecule drugs to pharmacologically-relevant protein receptors. Work will be conducted in collaboration with researchers at the Department of Medicinal Chemistry.
Supervisor: Kasper D. Rand.
No of students: 1-2

New agents for disulfide-bond reduction of therapeutic proteins
Biomolecules are versatile and highly potent candidates for new drugs (biopharmaceuticals). Often naturally occurring proteins contain covalent modifications  (glycosylations, disulfide bonds) which can render them difficult to analyze. In this project, you will design and test the potential of new chemical agents for efficient removal (reduction) of disulfide bonds in proteins. You will learn how to couple liquid chromatography with MS analysis to monitor the chemical reaction and how to identify protein modifications by MS.  Promising new agents for chemical reduction of protein disulfide bonds will be optimized and tested on proteins of particular biopharmaceutical potential, including recombinant antibodies and proteolytic enzymes. If successful, the protocol will possibly be applied and evaluated on the protein drug Coagulation Factor VIIa (NovoSeven) in collaboration with Novo Nordisk A/S.
Supervisor: Kasper D. Rand.
No of students: 1-2