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Ph.D., Chemical Engineering, University of Delaware, 2003
B.S., Chemical Engineering, University of Maine, 1998
Tessier joined RPI in 2007 after completing a postdoctoral fellowship in Susan Lindquist’s lab at the Whitehead Institute for Biomedical Research (MIT).
Tessier has received several awards, including two prestigious postdoctoral fellowships, one from the American Cancer Society (accepted) and another from the National Institutes of Health (declined by PMT), a National Aeronautics and Space Administration graduate research fellowship and the W. H. Peterson Award from the Biochemical Technology division of the American Chemical Society.
The Tessier lab seeks to integrate aspects of chemical engineering (solution thermodynamics, colloidal and interface science) and molecular/cellular biology to provide new fundamental insights into the misfolding and aggregation of proteins, a problem of profound importance to our society. Many neurodegenerative diseases are caused by aberrant protein folding and aggregation. Moreover, the efficacy of many protein therapeutics is limited due to their propensity to aggregate during bioprocessing, storage and delivery. The Tessier lab is interested in employing a variety of established and novel biophysical methods to uncover and understand the molecular interactions that drive protein aggregation. A working hypothesis of the lab is that relatively small regions of sequence within proteins govern their aggregation and that the identification and analysis of these sequence elements can provide important molecular-level insights into protein aggregation and potential therapeutic strategies to inhibit this process.
Tessier’s lab is particularly interested in the formation of highly ordered, beta-sheet rich amyloid fibers. Prions are a particularly interesting class of amyloid-forming proteins that are studied in the lab. These infectious proteins have received much public attention given their unique ability to transmit their beta-sheet rich, prion conformations from cell-to-cell and, in some cases, between different organisms (e.g., as in mad cow disease). The lab studies naturally occurring prions in yeast to understand several fundamental questions in prion biology ranging from how these proteins assemble into different amyloid conformations (protein strains) to how they cross species barriers.
The Tessier lab is also interested in the aggregation of Abeta into soluble oligomers and insoluble fibers given the importance of these toxic conformers in Alzheimer’s disease. The lab is developing new assays for understanding mechanisms of small molecule antagonism of Abeta aggregation. Moreover, in collaboration with Jon Dordick, the lab is synthesizing novel anti-aggregation compounds biocatalytically and evaluating mechanisms by which these compounds disrupt Abeta assembly.
A third area of interest to the lab is monoclonal antibody aggregation, a problem of significant importance to the biopharmaceutical industry. The stability of antibodies, especially at high concentrations necessary for formulation and delivery (10-100 mg/mL), is governed both by conformational stability (resistance to unfolding) and colloidal stability (resistance to intermolecular association between natively or near-natively structured proteins). Much effort has been focused on improving antibody conformational stability while very little effort has focused on the selection of antibodies with improved colloidal stability. Therefore, the Tessier lab is currently developing nanoparticle-based, highly efficient screens to assay antibody colloidal stability to aid in the design and selection of aggregation-resistant antibodies.
Tessier, P.M., Jinkoji, J., Cheng, Y.-C., Prentice, J.L., Lenhoff, A.M., “Self-interaction nanoparticle spectroscopy: A nanoparticle-based protein interaction assay”, J. Am. Chem. Soc., published online Feb 14th (2008).
Tessier P.M., Lindquist S., “Prion recognition elements govern nucleation, strain specificity and species barriers”, Nature, 447, 557 (2007). See accompanying commentaries in Nature, 447, 541(2007), Nat. Methods, 4, 538 (2007) & J. Cell Biol., 177, 747 (2007).
Tessier, P.M., Sandler, S.I., Lenhoff, A.M., “Direct measurement of protein osmotic second virial cross coefficients by cross-interaction chromatography”, Protein Sci., 13, 1379 (2004).
Tessier, P.M., Johnson, H.R., Pazhianur, R., Berger, B.W., Prentice, J.L., Bahnson, B.J., Sandler, S.I., Lenhoff, A.M., “Predictive crystallization of ribonuclease A via rapid screening of osmotic second virial coefficients,” Proteins, 50, 303 (2003).
Tessier, P.M., Lenhoff, A.M., “Measurement of protein self-association as a guide to crystallization,” Curr. Opin. Biotechnol., 14, 512 (2003).
Tessier, P.M., Verruto, V.J., Sandler, S.I., Lenhoff, A.M., “Correlation of diafiltration sieving behavior of lysozyme-BSA mixtures with osmotic second virial cross coefficients”, Biotechol. Bioeng., 87, 303 (2003).
Tessier, P.M., Lenhoff, A.M., Sandler, S.I., “Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography,” Biophys. J., 82, 1620 (2002).
Tessier, P.M., Vandrey, S.D., Berger, B.W., Sandler, S.I., Lenhoff, A.M., “Self-interaction chromatography: A novel screening method for rational protein crystallization,” Acta Cryst. D, 58, 1531 (2002).
Tessier P.M., Christesen S.D., Ong K.K., Clemente E.M., Lenhoff A.M., Kaler E.W., Velev O.D., “On-line spectroscopic characterization of sodium cyanide with nanostructured gold SERS substrates,” Appl. Spectrosc., 56, 1524 (2002).
Tessier P.M., Velev O.D., Kalambur A.T., Lenhoff A.M., Rabolt J.F., Kaler E.W., “Structured metallic films for optical and spectroscopic applications via colloidal crystal templating,” Adv. Mater., 13, 396 (2001).
Tessier P.M., Velev O.D., Kalambur A.T., Rabolt J.F., Lenhoff A.M., Kaler E.W., “Assembly of gold nanostructured films templated by colloidal crystals and use in surface-enhanced Raman spectroscopy,” J. Am. Chem. Soc., 122, 9554 (2000).
Velev O.D., Tessier P.M., Lenhoff A.M., Kaler E.W., “A class of porous metallic nanostructures,” Nature, 401, 548 (1999).
Contact Information:
Peter Tessier
(518) 276-2045
tessier@rpi.edu
www.rpi.edu/~tessip
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