Freeze-dryer console

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One of our key objectives is to develop robust synthetic methodologies that are amenable to high throughput parallel synthesis of compounds that will serve as tools in investigations of complex networks of bimolecular interactions. Currently, we are focusing on the design and synthesis of heterocyclic and peptidomimetic scaffolds that can selectively modulate the catalytic activity of human farnesyl pyrophosphate synthase (hFPPS) in vitro, in cell-based assays and in animal models. The hFPPS enzyme occupies a strategic location at the first committed step of the mevalonate pathway leading to protein prenylation of the Ras oncogenic proteins. In addition, this enzyme is implicated in the interferon-induced innate immune response against viral infections in humans. Therefore, hFPPS plays a crucial role at a cross-over point between the host's metabolism, oncogenesis and innate immunity. Studies in this area require the synthesis of numerous compounds which must be purifies by reversed phase HPLC and subsequently lyophilized to dryness. The requested Freeze-Dryer instrument is a key component within a cluster of instruments required for the success of our research program. This cluster of instruments is essential in achieving the efficiency and throughput of compound preparation that is needed in order to thoroughly investigate the interactions between hFPPS and its active site inhibitors, as well as the interactions between hFPPS and the host factor viperin, in vitro and in cell-based biological assays.