Matthew B. Soellner

Assistant Professor of Medicinal Chemistry

Ph.D., University of Wisconsin-Madison
Postdoctoral Fellow, University of California, Berkeley

Research Focus: Kinase inhibitors; Protease substrates/inhibitors; Peptidomimetics

Phone: 734.615.2767      
E-mail: soellner@umich.edu

Selective Protease Substrates.
Proteases, which catalyze the hydrolysis of amide bonds in peptides and proteins, play essential roles in most biological processes and are very important therapeutic and diagnostic targets for a multitude of diseases, including cancer. Efficient and systematic combinatorial tools will be developed to determine the substrate specificity profiles of proteases involved in prostate cancer. Generation of completely selective substrates for prostate cancer proteases will aid in designing more selective diagnostic tools in addition to serving as a basis for protease inhibitor design.

Substrate-competitive Kinase Inhibitors.
Protein Tyrosine Kinases (PTKs) are a major contributor to oncogenesis. Over the past decade, much attention has been focused on the development of ATP-competitive inhibitors from both academia and the pharmaceutical industry. Methodology for the generation of substrate-mimetic inhibitors of PTKs will be developed using novel fragment-based high throughput screening methods. Inhibitors that bind in the substrate pocket of a target kinase could help positively address potential issues with modern ATP-competitive inhibitor development, namely selectivity and susceptibility to resistance.

Peptidominetics for Disruption of Protein-Protein Interactions.
Utilizing a novel oligomeric structure, peptidomimetics that adopt helical conformations (foldamers) will be synthesized and evaluated for the targeted disruption of protein-protein interactions involved in oncogenesis.

Soellner Research Group


National Institutes of Health, Pathway to Independence Award
National Institues of Health, Ruth Kirschstein Postdoctoral Fellowship

Representative Publications

  1. Soellner, M.B., Rawls, K.A., Grundner, C. Alber, T., Raines, R.T., "Fragment-based substrate activity screening method for the identifications of potent inhibitors of the Mycobacteriym tuberculosis phosphatase PtpB", J. Am. Chem. Soc., 2007, 129, 9613.

  2. Tam, A., Arnold, U., Soellner, M.B., Raines, R.T., "Protein prosthesis: 1,5-Disubstituted-[1,2,3]-triazoles as cis peptide bond mimics", J. Am. Chem. Soc., 2007, 129, 12670.

  3. Maniere, Moore, M.E., Soellner, M.B., Tsang, P., Caperelli, C.A., "Human glycinamide ribonucleotide transformylase: active site mutants as mechanistic probes", Biochemistry, 2007, 46, 146.

  4. Soellner, M.B., Tam, A., Raines, R.T., "Staudinger ligation of peptides at non-glycyl residues", J. Org. Chem., 2006, 71, 9824.

  5. Soellner, M.B., Nilsson, BlL. Raines, R.T., "Reaction mechanism and kinetics of the traceless Staudinger ligation", J. Am. Chem. Soc., 2006, 128, 8820.