Molecular Interactions and NMR

Our research uses spectroscopic methods (especially NMR) to probe the molecular basis of interactions between molecules.

Head of Laboratory

Research Interests

Transfer-NMR (TR-NMR) experiments are at the heart of our research. TR-NMR can specifically provide the spectrum of a ligand that binds to a biomolecule (diffusion NMR / DOSY). Saturation Transfer Difference (STD) NMR gives us the interaction surface for the bound molecule. Transfer nuclear Overhauser effect spectroscopy (TR-NOESY) gives us the bound conformation around flexible bonds. DOSY and STD can extract information for bound ligands in the presence of a mixture of non-binding ligands. TR-NMR is used to screen small molecule libraries (pharmaceutical applications) and to investigate specific ligands (biochemical applications). Our research can be summarized as:

• Application of standard TR-NMR methods to interesting systems supplied by collaborators, e.g. lectin-carbohydrate interactions (1)
• Application of standard methods to novel biomolecules or ligand classes, e.g. DNA or extracellular proteins as targets, or the selection of the most appropriate fluorescent ligand analog to characterize a protein by fluorescent methods
• To develop new TR-NMR protocols and experiments (2), e.g. the screening of a peptide library (generated from a protein by proteolysis) against its protein target
• To characterize EF-hand, calcium-binding proteins and to use them as model TR-NMR systems (3)

To achieve these goals, we make extensive collaborations with researchers at the ITQB and throughout Europe.

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Selected Publications

1. M. Politi, J. Alvaro-Blanco, P. Groves, A. Prieto, J.A. Leal , F.J. Cañada and J. Jiménez-Barbero (2006)  Screening garlic water extract for binding activity with Cholera Toxin B pentamer by NMR. An old remedy giving a new surprise. European Journal of Organic Chemistry, 2067-2073.
2. K.E. Kövér, P. Groves, J. Jiménez-Barbero and G. Batta (2007)  Molecular recognition and screening using STD NMR:  15N-group selective STD NMR experiment to study intermolecular interactions in heavily overlapped spectra.  Journal of the American Chemical Society, 129, 11579-11582.
3. M. Palczewska, G. Batta, P. Groves, S. Linse, and J. Kuznicki (2005 ) Localization of the Ca(2+)- and H(+)-dependent hydrophobic properties of calretinin. Protein Science, 14, 1879-1887.

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Laboratory's Website

The group belongs to CERMAX

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