Drug and Ligand Binding (Functional Genomics and Interactome)
The study of molecular interactions is an exponentially growing area in the field of structure-function relationships of biologically important molecules. On the molecular level, biological activity corresponds to the binding of a substrate, inhibitor, drug (low molecular weight) to a macromolecular receptor, usually a protein.
CD is the ideal technique to determine the binding affinity and the ability to monitor a wide spectral region (140-700nm) enables the researcher to choose the appropriate region. The advantage of CD spectroscopy is that it measures the molecular binding affinity directly, without labelling or immobilising any of the ligand/receptor components and using small amounts of material.
The function and activity of a protein depends primarily on its 3D structure. The understanding of protein folding dynamics is a prerequisite for modelling confidently the native protein structure from the amino-acid sequence. Crystallisation condition induces conformation to samples of interest and understanding the changes may lead to better crystallisation procedure. The combination of simulated and observed electronic CD, vibrational CD and ROA spectra is going to be a powerful tool to address correctly the protein folding.
There is a growing interest in the structure-function relationship of nucleic acids with ligands, in particular for anti-cancer and anti-viral applications.
Nanoparticles are widely used as possible candidates in biosensor and drug delivery. Little is known of its properties on adsorbed samples. Possible conformational changes due to sample adsorbed on the surface can now be monitored by SRCD due to its highly collimated microbeam. This allows highly adsorbing nanoparticles to be monitored of any changes to the sample it is adsorbed on. This is useful in determining if there is any effect on toxicology properties of the adsorbed sample as well as possible use as biosensor.