High Speed Deuterium Exchange Mass Spectrometry and Related Technologies
Non-exclusive licensing of issued patents and published patent applications are now available on a yearly fee basis. Issued patents may be licensed for one year for $10,000, while published patent applications may be licensed for one year for $7,500.
Research associated with the technology and the general field can be reviewed in these publications:
The available technologies include:
SD2002-108 “Improved High Throughput Deuterium- Exchange- Mass Spectroscopic (HT-DXMS)- Methods for the Characterization of Protein Structure, Dynamics, and Binding Interactions”
Investigators at UC San Diego have invented improved methods whereby High Throughput- Deuterium Exchange Mass Spectroscopy (HT-DXMS) can be used to rapidly characterize, at the amino acid residue level, protein structural stability, dynamics, and binding interactions with other proteins or small molecules. Amide or alkyl(side chain) hydrogen- deuterium exchange is performed to label functionally important residues in the protein of interest, and then the location of label is rapidly and precisely determined with the invention. This method is simpler, faster and offers higher throughput than previous methods, which either result in low-resolution localization of the label or require multiple rounds of proteolytic degradation of labeled protein. The method is especially adapted to utilize data acquired and processed by existing high-throughput instrumentation, chemistries, and software recently developed at UC San Diego.
U.S. patent application number: 10,510,775
SD2002-157 “The Use Of Deuterium Exchange-Mass Spectrometry To Enhance Large-Scale Protein Crystallographic Structure Determination”
Investigators at UC San Diego have invented improved methods whereby deuterium exchange mass spectrometry can be used to enhance and guide large-scale protein crystallographic structure determination. High throughput crystallographic protein structure determination would be considerably facilitated by the ability to rapidly and precisely define structured/unstructured regions of a target and then use this information to produce constructs containing the structured regions in unaltered conformation, but otherwise depleted of unstructured regions. A large body of theoretical and experimental work has established that, in a folded protein, each peptide amide’s exchange rate with solvent hydrogen reports the protein’s thermodynamic stability at the individual amino acid scale. The invented method can specifically target structured/disordered regions of target proteins and be used to speed protein crystallographic structure determination. The method is especially adapted to utilize data acquired and processed by existing high-throughput instrumentation, chemistries, and software recently developed at UC San Diego. It is anticipated that this method can save both time and money in the high-throughput determination of protein structure for drug discovery.
SD2003-105 “High Throughput Protein 3D Structure Determination Employing Enhanced Amide Deuterium Exchange Mass Spectrometry (DXMS)”
UC San Diego researchers have invented a technique for high resolution 3D protein structure determination that breaks through the limitations presented by crystallographic and NMR- based techniques. The method uses rapidly acquired, high resolution amide deuterium exchange- mass spectrometric (DXMS) experimental data, obtained from microgram quantities of soluble protein, to provide constraints sufficient to determine a protein's high resolution 3D structure. It is especially adapted to utilize data acquired and processed by existing high-throughput instrumentation, chemistries, and software ("DXMS") recently developed at UC San Diego.
U.S. patent application number: 10,577,179
SD2003-107 “Method for High Throughput Improvement in Protein Crystallizability for 3D Structure Determination”
Investigators at UC San Diego have invented methods whereby deuterium exchange mass spectrometry can be used to markedly improve the crystallizability of target proteins. The method may make the majority of target proteins amenable to high throughput crystallographic analysis for 3D structure determination, on a large scale. It is especially adapted to utilize data acquired and processed by existing high-throughput instrumentation, chemistries, and software ("DXMS") recently developed at UC San Diego. The method can specifically target disordered regions of target proteins, inducing them to form their functionally appropriate 3D structures. This facilitates protein crystallization, and allows determination of the functional structure of such otherwise disordered regions of the protein. It is anticipated that this method can save both time and money in the high-throughput determination of protein structure for drug discovery.
Keywords: crystallography, mass spectrometry, mass spec, protein analysis, drug discovery
Case Numbers: SD2002-108, SD2002-157, SD2003-105, SD2003-107
Inquiries To: invent@ucsd.edu