This action funds the existing Industry/University Cooperative Research Center for Biomolecular Interaction Technologies at the University of New Hampshire for the final phase. The Center fosters the development of innovative laboratory instruments and methods for use in pharmaceutical research. The continued growth of the pharmaceutical and biotech areas can be helped by developing more efficient instrumentation that characterizes biomolecules for the synthesis and extraction of new compounds.
BITC’s mission statement ? To provide advanced methods for the analysis of biomolecular Interactions, to transfer technologies through training, consultation and Collaboration, to provide an environment in which academic and industrial researchers interact ? To fulfill this mission, BITC: Funds the development of novel instruments and methods, evaluates the usefulness of new technologies, trains students, post docs and researchers on new instruments and Methods, provides workshops, round table discussions and web-based resources. BITC Distributed over $3 million for research, funded 30 different research projects, generated over 70 proposals for funding, obtained $225,000 in supplemental NSF grants. Funded BITC research projects ? Capture and reconstitution of G-protein coupled receptors on biosensor surfaces. University of Utah. ? High-throughput, high-precision absorbance data acquisition for the analytical ultracentrifuge. CAMIS. ? Construction of a prototype fluorescence detector for the analytical ultracentifuge. CAMIS. ? Analytical Ultracentrifugation as a method for identifying and characterizing Src-containing multi-protein complexes in cancer cells. St. Anselm College, NH. ? Testing, validation and assay development for a new coupled plasmon waveguide resonance biosensor. University of Utah ? Development of software for real-time display and analysis of sedimentation velocity software. Boston Biomedical Research Institute ? Web based computer aided interpretation of analytical ultracentrifugation data. BBRI. ? Detection of protein binding and protein conformational changes by surface plasmon coupled emission. ? Interaction of a stathmin-GFP construct with tublin and tublin-fluorescence by absorbance and fluorescence analytical ultracentrifugation. U. of Mississippi. ? Applications of atomic force microscopy for the analysis of biomolecular interations. U. of Miami ? Quantitative FRET microscopy measurement of protein-protein interactions in vivo. Clemson University. ? Multiplexed quantitation and screening via flow cytometry protein interaction assay (FCPIA), U. of Michigan. ? Rapid Ultrasensitive Biochemical Detection Based on Fiber Optics Surface Plasmon- Coupled Emission (POSPCE), UNH, Univ. of N. Texas. ? A Disposable Polymeic Microdevice for Energetic Characterization of Biomolecular Interactions,Columbia. ? Cause, Consequence and Manipulation of mAb Valence, Univ. of NH. ? A novel calorimetric assay for the study of drug-plasma protein interactions, Univ. of Louisville. ? Detected mAb aggregates in serum, Univ. of NH. ? Sednterp, Univ. of NH ? Interpreting fluorescence detected sedimentation for mAb interactions in serum. Univ. of NH. ? Brewster angle straddle interferometry for high throughput binding assays. Univ. of Rochester. ? Evaluation of a Commercial Membrane Confined Electrophoresis Device, Univ. of NH. ? A High Precision Vapor Pressure Osmometer for Investigating Biomolecular Interactions, Univ. of Connecticut Health Center, Farmington CT. ? Origin of Altered Thermograms in Plasma from Diseased Individuals, Univ. of Louisville. ? Microfluidic Characterization of Sub-Visible Particles, North Carolina State University ? Dynamic Modeling of Protein-Protein Interactions in High Concentration Biological Systems, University of New Hampshire ? Characteristics and applications of membrane nanodiscs, University of New Hampshire ? Quantitative high-throughput structural mapping of protein-protein reactions by hydroxyl radical ‘foot printing’, Albert Einstein College of Medicine ? High-throughput analysis of antibody interactions in serum, Rensselaer Polytechnic Institute ? A simple device for dipole estimation, University of New Hampshire ? The role of charge in blood coagulation initiation, University of New Hampshire BITC-supported instrument commercialization ? A fluorescence detection optical system (AU-FDS) ? Licensed by Aviv Biomedical, Inc. ? Over 30 AU-FDS units have been installed in 6 years ? Several at BITC companies. ? A membrane confined electrophoresis (MCE) instrument ? Developed by Spin Analytical. Inc., - a startup company founded in response to BITC member company needs. ? Sample holders and an automated cell washer ? Licensed from UNH by Spin Analytical, Inc. ? Specialty tools and new tool designs ? Developed by Spin Analytical with discounted sales to BITC member companies. Novel instruments and methods Atomic force microscope force measurements of biological interactions U. Miami A surface plasmon-coupled fluorescence emission detector for characterization of protein-protein interactions, at the U. of North Texas, a version built at UNH Protein charge determination using membrane confined electrophoresis (MCE). UNH A high-sensitivity, high-precision vapor pressure osmometer. UConn Differential scanning calorimetry drug binding to plasma proteins. U. of Louisville Brewster straddle-angle interferometry for binding assays. U. of Rochester Microfluidic characterization of sub-visible particulates. NC State Charge measurement of apo- and holo- lipid nanodiscs. UNH Development of methods to determine monoclonal antibody charge. UNH. Src-Containing Protein Complexes in Mammalian Cell Lysates. St. Anselm College Methods to obtain thermodynamic information from AU-FDS. U.Miss.Med.Ctr. Quantitative FRET measurements of protein-protein interactions in vivo. Clemson U. Quantitation and screening of protein interactions via flow cytometry. U. Mich. A Disposable chip micrcalorimeter. Columbia U. Detection of monoclonal antibody interactions in serum. UNH Software development ? Data acquisition and analysis software for the AU-FDS (AOS 1.0 – 1.8). UNH ? Analytical electrophoresis interpretation (ZUtilities). UNH ? Web-based and desktop sedimentation interpretation (Sednterp 3.0). UNH ? Real-time g(s) analysis of sedimentation velocity (Sedview 1.1). BBRI ? Brownian dynamic simulation of high-concentration antibody solutions. UNH
