- Undergraduate Education
- B.A St. Louis University (1980)
- Graduate Education
- Ph.D. Washington University, St. Louis (1987)
- Postdoc. Washington University, St. Louis (1987-89)
- Professor. Albert Einstein College of Medicine
- Joined Texas A&M in 1996
Crystallography / Drug Design
My lab uses X-ray crystallography to better understand the relationship between proteins and ligands. Tiny differences in the structure of a molecule can radically change the interaction between a protein and ligand and we are only begining to understand how many factors play a role in this interaction. By manipulating the individual components of a compound it is possible to create a chemical that binds to the protein better than the natural substrate, and prevent the natural reaction from occurring. This is the basis for rational drug design. Our efforts have lead us to collaborations with other labs and scientists in many disciplines as our approach to directed compound design has applications not only in basic research but also in pesticide development, health research and clinical research.
Puckett, S, Trujillo, C, Wang, Z, Eoh, H, Ioerger, TR, Krieger, I et al.. Glyoxylate detoxification is an essential function of malate synthase required for carbon assimilation in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 2017;114 (11):E2225-E2232.
Zhu, M, Harshbarger, WD, Robles, O, Krysiak, J, Hull, KG, Cho, SW et al.. A strategy for dual inhibition of the proteasome and fatty acid synthase with belactosin C-orlistat hybrids. Bioorg. Med. Chem. 2017; :.
Gomez, JE, Kaufmann-Malaga, BB, Wivagg, CN, Kim, PB, Silvis, MR, Renedo, N et al.. Ribosomal mutations promote the evolution of antibiotic resistance in a multidrug environment. Elife. 2017;6 :.
Huang, HL, Krieger, IV, Parai, MK, Gawandi, VB, Sacchettini, JC. Mycobacterium tuberculosis Malate Synthase Structures with Fragments Reveal a Portal for Substrate/Product Exchange. J. Biol. Chem. 2016;291 (53):27421-27432.
Park, Y, Pacitto, A, Bayliss, T, Cleghorn, LA, Wang, Z, Hartman, T et al.. Essential but Not Vulnerable: Indazole Sulfonamides Targeting Inosine Monophosphate Dehydrogenase as Potential Leads against Mycobacterium tuberculosis. ACS Infect Dis. 2017;3 (1):18-33.
Palencia, A, Li, X, Bu, W, Choi, W, Ding, CZ, Easom, EE et al.. Discovery of Novel Oral Protein Synthesis Inhibitors of Mycobacterium tuberculosis That Target Leucyl-tRNA Synthetase. Antimicrob. Agents Chemother. 2016;60 (10):6271-80.
Martínez-Hoyos, M, Perez-Herran, E, Gulten, G, Encinas, L, Álvarez-Gómez, D, Alvarez, E et al.. Antitubercular drugs for an old target: GSK693 as a promising InhA direct inhibitor. EBioMedicine. 2016;8 :291-301.
Bhatt, VS, Zeng, D, Krieger, I, Sacchettini, JC, Cho, JH. Binding Mechanism of the N-Terminal SH3 Domain of CrkII and Proline-Rich Motifs in cAbl. Biophys. J. 2016;110 (12):2630-41.
Almeida, D, Ioerger, T, Tyagi, S, Li, SY, Mdluli, K, Andries, K et al.. Mutations in pepQ Confer Low-Level Resistance to Bedaquiline and Clofazimine in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 2016;60 (8):4590-9.
Guardia, A, Gulten, G, Fernandez, R, Gómez, J, Wang, F, Convery, M et al.. N-Benzyl-4-((heteroaryl)methyl)benzamides: A New Class of Direct NADH-Dependent 2-trans Enoyl-Acyl Carrier Protein Reductase (InhA) Inhibitors with Antitubercular Activity. ChemMedChem. 2016;11 (7):687-701.