Cees Gooijer opent The Analytical CHallenge 2010
Hoogleraar Applied (Laser) Spectroscopy aan de Vrije Universiteit van Amsterdam, Cees Gooijer, geeft de plenaire openingslezing op eerste dag (1 november) van de Analytical Challenge 2010. Gooijer zal spreken over Trusting back Fontiers of Analytical Biomolecular Spectroscopy. Aanvang: 10.00 uur.
Summery
It is the challenge of analytical biomolecular spectroscopy to develop and implement analytical methodologies directed at the detection and structural characterization of biologically active molecules. To fully characterize such molecules, eventually not only the molecular properties as such are important, but also the (stereo selective) dynamic interaction with their immediate environment.
Molecular spectroscopy methods are widely involved in this field, in particular absorbance and fluorescence spectroscopy. Unfortunately, the former one has a limited sensitivity, while the latter one – though providing excellent sensitivity and better selectivity than absorbance – is characterized by a low spectral resolution. The other mode of molecular luminescence with a high analytical potential, i.e. molecular phosphorescence is hardly invoked yet; it is generally seen as not being applicable to liquid solutions. Furthermore, Raman Spectroscopy (RS), the vibrational technique of choice for aqueous samples, is still scarcely playing a role in analytical biomolecular spectroscopy. As a technique based on inelastic scattering, it suffers from a poor sensitivity so that (too) high analyte concentrations are needed; furthermore in practice RS spectra are frequently overwhelmed by fluorescence.
In this presentation we will briefly discuss recent achievements in our group (supervised by Dr. Freek Ariese and Dr. Gert van der Zwan), directed on thrusting back the frontiers of the above molecular spectroscopy methods: A laser-based alternative absorbance detection method, i.e. Cavity Ring Down Spectroscopy in the evanescence mode to directly monitor the adsorption of protein (monolayers) to capillary walls, a main point of concern in protein capillary electrophoresis (CE). High-resolution fluorescence to study the structure of ligand-receptor complexes. Room temperature phosphorescence as a sensitive detection method for CE providing enantioselectivity based on phosphorescence lifetimes.
By using Resonance Raman Spectroscopy in the deep-UV the RS sensitivity limitation is largely tackled. Furthermore we have successfully involved a combined electrochemistry-Resonance Raman Spectroscopy approach to obtaine detailed information about redoxprotein-ligand interactions. Last but not least we are currently developing time-gated RS, enabling the recording of RS of fluorescent proteins. Fascinating is the possibility to use it for depth profiling purposes by making use of differences in photon travelling times.
