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JDurant2005
JD,TM,JK
Assistant Research Professor Jennifer Durant (left) with Research Professor Tom Moody (right) and M.S.  student Jon Kingsbury (center).

Jennifer A. Durant


Research Assistant Professor
Biochemistry and Molecular Biology

University of New Hampshire
Rudman Hall 385
46 College Road
Durham NH 03824

Tel.Office (603) 862-4316
Tel. Lab   (603) 862-1696
E-mail: jennifer.durant@cisunix.unh.edu

PROFILE
Protein biochemist with 2 years of postdoctoral experience in both academic and industry directed projects.  Have personally worked with 12 different proteins and peptides employing a wide variety of biophysical and biochemical methods including ATR-FTIR, AUC, HPLC/LS, CE, MCE, SPR and MS.  Have recently gained experience in microfluidic technology.  My interests focus on the application of biophysical techniques to solve or advance medically related issues such as oral delivery of protein and peptide therapeutics.

RESEARCH EXPERIENCE
Univiersity of
New Hampshire, Research Faculty                                         (Sept 2005 - Present)
Project1:  Development of Nanovesciles for Oral Delivery of Therapeutics
Working with Jerome Claverie (Materials Science Program, UNH) and Bentley Pharmaceuticals (Exeter, NH), we are characterizing nanovesicles and their drug transport properties.  We are using Caco-2 cell monolayers as a permeability model and a number of biophysical techniques, including ATR-FTIR, AUC-FDS, and CE,  in our efforts to optimize the delivery system.
University of New Hamphsire, Post Doctoral Fellow                               (May 2003 – Sept 2005)     
Project 1: Development of a microfluidic electrophoresis device with multiple wavelength fluorescence detection for early stage cancer diagnosis.
Sentry Biosciences, Inc. – contact Diane Kozwich and Charlie Barnett  (Feb2005-Aug2005)

    A microfluidic device was constructed and tested with a model system (GFP) to determine the feasibility of rapid testing (<1hr) for trace amounts of cancer markers in crude samples such as blood.  We  worked with PDMS for rapid prototyping and are collaborating with the University of Maine LASST center (Professor Rosemary Smith) for the photolithography aspects.  Our eventual target molecule is currently osteopontin.

Project 2:  Development of a web based technical resource center for new industry scientists
Biomolecular Interaction Technologies Center (BITC) – contact Michelle Gregoire  (2004-present)
    Designed, assembled, and wrote material for a web based resource to help new scientists quickly understand and identify potentially useful biophysical characterization techniques.  Currently covers 16 different instruments including new technologies such as resonant acoustic profiling (RAP) and surface plasmon coupled emission.  Responsible for updating and adding the newest technologies as they become available.

Project 3:  Determination of the  valence of activated drotrecogin alfa (activated protein C)   
Elli Lilly – contacts Cassandra Fletcher and Brian Matthews  (2003 – July2005)
    Measurement of the hydrodynamic radius of activated protein C was made both by analytical ultracentrifugation (sedimentation velocity) and by dynamic light scattering.  This is used along with membrane confined electrophoresis (MCE) and capillary electrophoresis (CE) measurements to determine estimates of the electrostatic self-potential energy as function of Ca2+ concentrations.  Responsible for generation and submission of reports.

Project 4:  Investigate application of electrophoretic theories to large, nonglobular proteins.
CAMIS – contact Thomas Laue  (2003-2004)

    Hydrodynamic and electrophoretic measurements of both lysozyme and an N-terminally PEGylated lysozyme where made.  These measurements were used to determine the applicability of models to large, flexible macroions  in order to determine valence.

Project 5: Characterization of insulin fibrillation
Bentley Pharmaceuticals – contact Bob Gyurik  (Aug2004-Jan2005)

    Highly concentrated pharmaceutical preparations where characterized by ATR-FTIR to demonstrate the reversibility of insulin fibril formation.  Kinetic assays were also performed using fluorescence measurements and the fibril-binding dye thioflavin T.  Molecular weight determinations were made using analytical ultracentrifugation and CE was used to detect the prescence of desamido-insulin in the preparations.








 

The Center to Advance Molecular Interaction Sciences
University of New Hampshire
Durham, NH 03824
(603) 862-2459