Faculty & Staff bios

Peter Oelschlaeger, PhD, MS

Associate Professor of Pharmaceutical Sciences

College of Pharmacy

E-Mail: poelschlaeger@westernu.edu

Phone: 909-469-8232


2004 California Institute of Technology
2007 University of Southern California

PhD 2002 University of Stuttgart

MS 1999 University of Hohenheim

Research Interest

 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.

Research Grant

“Bicyclic beta-lactam antibiotics as poor substrates for metallo-beta-lactamases”
NIH-NIAID R15 Subcontract, PI: John D. Buynak, 2014-2017


Liu XL, Yang KW, Zhang YJ, Ge Y, Xiang Y, Chang YN, Oelschlaeger P.
Optimization of amino acid thioesters as inhibitors of metallo-beta-lactamase L1.
Bioorganic & Medicinal Chemistry Letters (2016), 26, 4698-71.

Nguyen TQ, Alqurafi M, Edwards C, Nguyen P, Kim J, Casco S, Bennet M, Chiang C, Lohry M, Cox M, Meshram B, Le D, Kim E, Smriti S, Oelschlaeger P, Buynak JD.
Functionalizing the γ-position of α-diazo-β-ketoesters.
Tetrahedron Letters (2016), 57, 3330-3.

Zhai L, Zhang YL, Kang JS, Oelschlaeger P, Xiao L, Nie SS, Yang KW.
Trazolylthioacetamide: a valid scaffold for the development of New Delhi Metallo-beta-lactamase-1 (NDM-1) inhibitors.
ACS Medicinal Chemistry Letters (2016), 7, 413-17.

LaCuran AE, Pegg KM, Liu EM, Bethel CR, Ai N, Welsh WJ, Bonomo RA, Oelschlaeger P
Elucidating the role of residue 67 in IMP-type metallo-beta-lactamase evolution.
Antimicrobial Agents and Chemotherapy (2015), 59, 7299-307.

Alsamarah A, LaCuran AE, Oelschlaeger P, Hao J, Luo Y
Uncovering molecular bases underlying bone morphogenetic protein receptor inhibitor selectivity.
PLoS ONE (2015), 10, e 0132221.

Oelschlaeger P, Aitha M, Yang H, Kang JS, Zhang AL, Liu EM, Buynak JD, Crowder MW
Meropenem and chromacef intermediates observed in IMP-25 metallo-beta-lactamase-catalyzed hydrolysis.
Antimicrobial Agents and Chemotherapy (2015), 59, 4326-30.

Liu XL, Shi Y, Kang JS, Oelschlaeger P, Yang KW
Amino acid thioester derivatives: a highly promising scaffold for the development of metallo-beta-lactamase L1 inhibitors.
ACS Medicinal Chemistry Letters (2015) 6, 660-664.

Yang SK, Kang JS, Oelschlaeger P, Yang KW
Azolylthioacetamide: a highly promising scaffold for the development of metallo-beta-lactamase inhibitors.
ACS Medicinal Chemistry Letters (2015), 6, 455-560.

Nguyen TQ, Chai W, Gu J, Cook K, Kim E, Goetz S, Farni Z, Chepuru M, Cox M, Nguyen P, Raja H, Magistrado P, Michael F, Oelschlaeger P, Buynak JD*
Triethylsilyl enol ethers in the synthesis of carbapenem precursors.
Tetrahedron Letters (2015), 56, 3385-3389.

Zhang YL, Yang KW*, Zhou YJ, LaCuran AE, Oelschlaeger P, Crowder MW*
Diaryl-substituted azolylthioacetamides: inhibitor discovery of New Delhi metallo-beta-lactamase-1 (NDM-1)
ChemMedChem (2014) 9:2445-2448

Pegg KM, Liu EM, George AC, LaCuran AE, Bethel CR, Bonomo RA, Oelschlaeger P*
Understanding the determinants of substrate specificity in IMP family metallo-beta-lactamases: the importance of S262
Protein Science (2014) 23:1451-1460

Yang KW*, Fang L, Yang SK, Aitha M, LaCuran AE, Oelschlaeger P, Crowder MW*
New  beta-phospholactam as a carbapenem transition state analog: synthesis of a broad-spectrum inhibitor of metallo-beta-lactamases
Bioorganic and Medicinal Chemistry Letters (2013) 23:5855-5859

Monti S*, Corozzi A, Fristrup P, Joshi KL*, Shin YK, Oelschlaeger P, van Duin ACT, Barone V
Exploring the conformational and reactive dynamics of biomolecules in solution using an extended Version of the glycine reactive force field.
Physical Chemistry Chemical Physics (2013) 15:15062-15077

Pegg KM, Liu EM, LaCuran AE, Oelschlaeger P*.
Biochemical characterization of IMP-30, a metallo-beta-lactamases with enhanced activity toward ceftazidime.
Antimicrobial Agents and Chemotherapy (2013) 57:5122-5126

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

Oelschlaeger P.
Outsmarting metallo-beta-lactamases by mimicking their natural evolution. (Review)
J Inorg Biochem (2008) 102:2043-51