It is possible to prevent noneffective drugs from entering costly (pre-)clinical trials by gaining a better understanding of the underlying biological mechanisms of drug-protein targets and the mechanism of action of promising leads. We offer solutions that enable to directly observe complex dynamic molecular processes and identify the most promising leads.
Scientists can study how proteins interact with DNA or RNA molecules and visualize these interactions while correlating them with the mechanical properties of the system. In this way, they can characterize not only protein binding but also binding location and protein behavior after the binding, thus resolving the dynamics and functionality of the target. This additional information can help interpret the influence of different pharmaceuticals on the protein-DNA interactions to discover promising leads based on their MOA.
Scientists can use optical tweezers to trap beads and catch a biomolecule, such as a protein, in between. The folding and unfolding of the protein can then be monitored by moving the beads while measuring the force and extension. The combination of optical tweezers with simultaneous multicolor fluorescence measurements (e.g. with FRET) allows correlating the global mechanical properties of the protein with the local structural properties. With optical tweezers – fluorescence microscopy you can:
Scientists can use optical tweezers to trap beads and catch a biomolecule, such as DNA, in between, while an enzyme is interacting with it. It is then possible to study and quantify the effect of small molecules or biologics on the enzyme’s activity. The combination of optical tweezers with simultaneous multicolor fluorescence measurements allows correlating the mechanical properties of the DNA with the drug activity. With optical tweezers – fluorescence microscopy you can: