Peter Oelschlaeger, PhD, MS
Assistant Professor of Pharmaceutical Sciences
College of Pharmacy
Phone: 909-469-8232 |
PhD 2002 University of Stuttgart
MS 1999 University of Hohenheim
The general goal of research in my laboratory is to elucidate mechanisms of infectious diseases. In particular, we study bacterial antibiotic resistance conferred by metallo-beta-lactamases. The clinically most relevant of these enzymes are those of the IMP and VIM type, and more recently also NDM-1. We want to understand how these enzymes function and evolve under the selective pressure of antibiotics. In collaboration with other researchers in the field, we hope to discover more potent antibiotics and metallo-beta-lactamase inhibitors that can be given in combination with antibiotics. These could improve treatment while limiting the spread and evolution of metallo-beta-lactamases.
Liu EM, Pegg KM, Oelschlaeger P*
The sequence-activity relationship between metallo-beta-lactamases IMP-1, IMP-6, and IMP-25 suggests an evolutionary adaptation to meropenem exposure.
Antimicrobial Agents and Chemotherapy (2012) 56:6403-6406.
Widmann M, Pleiss J, Oelschlaeger P*
Systematic analysis of metallo-beta-lactamases using an automated database.
Antimicrobial Agents and Chemotherapy (2012) 56:3481-3491.
Xiong X, Bromley EH, Oelschlaeger P, Woolfson DN, Spencer J.
Structural insights into quinolone antibiotic resistance mediated by pentapeptide repeat proteins: conserved surface loops direct the activity of a Qnr protein from a Gram-negative bacterium.
Nucleic Acids Res (2011) 39:3917-3927
Tsang C, Malik H, Nassman D, Huang A, Tariq F, Oelschlaeger P, Stathopoulos C.
Intramolecular interactions between the protease and structural domains are important for the functions of serine protease autotransporters.
Infect Immun (2010) 78:3335-45
Oelschlaeger P, Ai N, DuPrez KT, Welsh WJ, Toney JH.
Evolving Carbapenemases: Can Medicinal Chemists Advance One Step Ahead of the Coming Storm? (Perspective)
J Med Chem (2010) 53:3013-27
Rucker R, Oelschlaeger P, Warshel A.
A binding free energy decomposition approach for accurate calculations of the fidelity of DNA polymerases.
Proteins (2010) 78: 671-80
Outsmarting metallo-beta-lactamases by mimicking their natural evolution. (Review)
J Inorg Biochem (2008) 102:2043-51