David H. Thompson

David H. Thompson Profile Picture

Professor - Organic & Biomolecular Chemistry
Colorado State University, Ph.D., Organic Chemistry, 1984

Contact Info:


Training Group(s):
Biomolecular Structure and Biophysics
Chemical Biology
Membrane Biology

Active Mentor - currently hosting PULSe students for laboratory rotations and recruiting PULSe students into the laboratory; serves on preliminary exam committees

Current Research Interests:

1. The Thompson Group is designing delivery strategies that mimic the endosomal uptake and acidification mechanism that many viruses exploit in their life cycle. The materials prepared in our lab e.g., lipids, lipopolymers, diblock copolymers and polyrotaxanes are endowed with sensitive functional groups within their structures that enable bioresponsive delivery from the carrier. Activation mechanisms utilized in our approach include endosomal acidification, oxidation, or enzymatic processes to degrade the carrier and improve the bioavailability and efficacy of the therapeutic cargo.

2. Integral membrane proteins (IMP) are an important class of biological targets for drug development because of the key roles they play in active transport, signal transduction, protein expression, energy generation/maintenance, and receptor-mediated responses to extracellular nutrients, drugs, and pathogens. IMP function is typically determined using whole cell or liposome assays, which are often imprecise, cumbersome, indirect, and lack sensitivity. Development of rapid and sensitive methods for assaying membrane protein function in planar sensor architectures is one of the major goals of this project, having broad practical and fundamental impact in the areas of drug discovery, mechanisms of membrane protein activity & hard-soft material interfaces in medical implants. We are currently focused on the membrane-associated enzyme, isoprenylcysteine carboxylmethyltransferase (ICMT), as our target for membrane sensor development. This work involves aspects of nanofabrication, chemical synthesis, surface analysis and the development of bioconjugation methods.

3. The long-term objective of our surface immobilization and Protein Crystallization, Ck is the development of rapid and general methods for generating interfaces that promote the assembly of proteins and protein complexes for rapid structural analysis. Our strategies are designed to utilize nitrilotriacetic acid-based material designs that are capable of binding to polyhistidine tags (his-tag) that are widely used for protein isolation and purification.

Selected Publications:

J. A. Boomer, M. M. Qualls, H. D. Inerowicz, R. Haynes, G. V. Patri, J.-M. Kim, D. H. Thompson, Cytoplasmic Delivery of Liposomal Contents Mediated by an Acid-Labile Cholesterol-Vinyl Ether-PEG Conjugate, Bioconjugate Chemistry 2009 20, 47-59.

S. Loethen, T. Ooya, H. S. Choi, N. Yui & D. H. Thompson, Synthesis, Characterization and pH-Triggered Dethreading of ±-Cyclodextrin Polyethylene Glycol Polyrotaxanes Bearing Cleavable Stoppers, Biomacromolecules 2006 7, 2501-2506.

G. Acharya, C.-L. Chang, D. Holland, D. H. Thompson, C. A. Savran, Rapid Detection of S-Adenosyl Homocysteine Using Self-Assembled Optical Diffraction Gratings, Angewandte Chemie, International Edition, 2008 47, 1051-1053.

W. Febo-Ayala, S. Morera-Felix, C. A. Hrycyna & D. H. Thompson, Functional Reconstitution of the Integral Membrane Enzyme, Isoprenylcysteine Carboxyl Methyltransferase, in Synthetic Bolalipid Membrane Vesicles, Biochemistry 2006 45, 14683-14694.

D. H. Thompson, M. Zhou, J. Grey, H.-k. Kim, Design, Synthesis and Performance of NTA-Modified Lipids as Templates for Histidine-Tagged Protein Crystallization, Chemistry Letters 2007 36, 956-975.

R. D. Wampler, D. J. Kissick, C. J. Dehen, E. J. Gualtieri, J. L. Grey, H.-F. Wang, D. H. Thompson, J.-X. Cheng, G. J. Simpson, Selective Detection of Protein Crystals by Second Harmonic Microscopy, Journal of the American Chemical Society 2008 130, 14076-14077.

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