Date:9/30/2011

r from the binding site, the higher is its own affinity for the target, and the more likely it is to be clinically effective. In the MS-based binding assay developed by Wanner's group, quantification of the marker is carried out using mass spectrometry. In contrast to conventional techniques, which employ radiolabeled ligands, MS binding assays do not require the use of markers containing radioactive isotopes. This means that the marker can be assayed in its unaltered, native state. "This label-free technique provides all the advantages offered by classical binding studies, while avoiding the need to work with radioactive compounds," explains Wanner. His team has now validated the MS-based binding assay for use in the search for new inhibitors of SERT function. "Because SERT regulates the concentration of serotonin in the synaptic cleft, the protein serves as the major target for the treatment of depression, obsessive-compulsive disorders and anxiety states," says Wanner. Using the well-known antidepressant (S)-fluoxetine as a native marker, his group has now shown that the results of the MS-based assay are in very good agreement with those obtained using radiolabeled ligands. Indeed, the team now routinely uses the MS method to screen for novel, pharmacologically active SERT inhibitors. In addition, Wanner has plans to adapt the approach for use with other target molecules of clinical interest. (gd)

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Contact: Dr. Kathrin Bilgeri kathrin.bilgeri@lmu.de 49-892-180-6938 Ludwig-Maximilians-Universitt Mnchen Source:Eurekalert

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