Associate Professor
I am in charge of the synthetic organic chemistry program within the Molecular Pharmacology Group at The Department of Medicinal Chemistry. The main emphasis of our research is the design and synthesis of new receptor ligands to be used as pharmacological tools for elucidating the function of receptors, their mechanism of activation etc. Our research falls into two distinct areas:
i) Synthesis of small molecules (Medicinal Chemistry)
ii) Synthesis of peptidomimetics / foldamers (Chemical Biology)
The research projects are carried out in close collaboration with computational chemists and pharmacologists within the group. Two examples of current research projects are described briefly below. Prospective students can read more about the group and our Medicinal Chemistry and Chemical Biology program by clicking here.
Potential national/international students are encouraged to contact me regarding joining the synthesis team (please allow up to one week for email responses).
In 2005 the Molecular Pharmacology Group cloned a novel G-protein coupled receptor termed GPRC6A. G-protein coupled receptors (GPCR) are implicated in many important physiological processes and it is likely that GPRC6A also regulates important physiological function(s) that are involved in pathophysiology. Using a combination of molecular modelling, pharmacology and medicinal chemistry, we are developing selective ligands for GPRC6A that allows us to perform detailed pharmacological studies of the receptor. Ultimately, we aim to initiate a drug discovery program targeting the pathophysiology associated with the receptor.

The aim of the β2 adrenergic receptor (B2AR) project is to gain a deeper understanding of the function and signalling of B2AR. We hope that new insights into B2ARs molecular mechanism of action will allow us to design allosteric modulators for B2AR with improved potency and selectivity.

B2AR was the first ligand-activated GPCR to be cloned. ß2AR is one of the most studied GPCRs in terms of determinants for orthosteric ligand binding, receptor activation and signalling. Recently, the crystal structure of ß2AR binding to the G-protein Gαs was reported by the laboratory of Brian Kobilka at Stanford University. Due to the available methods and detailed structural information for ß2AR, it represents a unique tool GPCR to study the molecular mechanisms of allosteric modulation and GPCR activation.
Our most recent publications can be found below. For a complete list of publications, including patents, popular science etc. click here.
Azide- and Alkyne-Derivatised alpha-Amino Acids, H. Johansson and D. Sejer Pedersen, Eur. J. Org. Chem., 2012, Accepted.
Selective inhibition of Biotin Protein Ligase from Staphylococcus aureus, T.P. Soares da Costa, W. Tieu, N.R. Pendini, M.Y. Yap, S.W. Polyak, D. Sejer Pedersen, R. Morona, J.D. Turnige, J.C. Wallace, M.C.J. Wilce, G.W. Booker, A.D. Abell, J. Biol. Chem., 2012, In Press.
1,2,3-Triazoles in Peptidomimetic Chemistry, D. Sejer Pedersen, and A.D. Abell, Eur. J. Org. Chem., 2011, 13, 2399-2411.

We are looking for students with an interest in organic synthesis / medicinal chemistry / chemical biology. If you think that a research project in our group could be something for you click here and read more.
Vist the Curly Arrow Chemistry Blog hosted by Mol. Pharm. Synthesis by clicking the image above.
Department of Medicinal Chemistry
Faculty of Pharmaceutical Sciences
Universitetsparken 2
2100 Copenhagen
Denmark
Phone: (+45) 353 36122
Fax: (+45) 35 33 60 41
E-mail: dsp(at)farma.ku.dk
Building 30, Room 344
University of Copenhagen
Faculty of Pharmaceutical Sciences
Universitetsparken 2
2100 Copenhagen
Denmark
Phone +45 35 33 60 00
Fax +45 35 33 60 01
Mail farma@farma.ku.dk
Web www.farma.ku.dk