Research Projects in Helena Danielson Group
The goal of our research is to extend our knowledge on how molecules interact with each other and how different properties of the molecules and their environment affect the interactions. This is important for understanding how biological processes are regulated and central to the development of new effective and safe drugs. Slight differences in the structure of a molecule can be decisive for its biological effect. Many diseases are caused by dysfunctional regulation of an important biological process arising as a result of structural changes in the molecules involved or their concentration at the site of action. Drugs are molecules that are specifically designed to interact with proteins that can correct such problems. If the organism that the molecule is intended to affect responds to the treatment by mutating, thereby changing the structure of the protein with which the molecule has been optimized to interact, the effect may be lost completely. It is the basis for a critical type of drug resistance that is particularly common in viruses.
We have established a unique competence on how biosensors can be used in drug development to analyze molecular interactions in detail. New methods and strategies are continuously being developed, and we have many collaborations with other research groups and companies interested in method development and the use of biosensors for interaction analyses. In addition, we are part of SciLifeLab's drug development platform where we assist their projects with experimental analyses. We have cutting-edge expertise in different types of biosensor technologies such as Biocore (Cytiva), Wave (Creoptix) and switchSENSE (Dynamic Biosensors), but also work with X-ray crystallography, enzyme analyses, molecular cloning, protein production and protein technology.
SMYD3 stands for SET and MYND-domain containing protein 3. The protein is a lysine methyltransferase that modifies histones and is involved in cancer and other epigenetically regulated diseases. We are interested in understanding the biological role of the protein in these processes via identification of novel non-active site targeting ligands.
You can read more about the project in our latest publication Discovery of an allosteric ligand binding site in SMYD3 lysine methyltransferase.
Conformational changes in ion channels
We study how ligand induced conformational changes in ligand gated ion channels occur and how gating is regulated.
You can read more about one of our most recent projects in the article Discovery of fragments inducing conformational effects in dynamic proteins using a second-harmonic generation biosensor.