John W. Tomsho, Ph.D.
John Tomsho PhD
Assistant Professor of Chemistry and Biochemistry
B.S. Pharmaceutical Chemistry, University of the Sciences in Philadelphia
Ph.D. Medicinal Chemistry, University of Michigan, Ann Arbor
- Developing new pharmaceutical agents for the treatment of diseases such as viral or bacterial infections and cancer
- Expanding the use of boronic acids as pharmaceutical agents
- Developing peptides for the disruption of protein-protein interactions
The development of new agents for the study and treatment of diseases is being pursued utilizing tools from the fields of chemistry and biology. The research in my group is currently focused on the development of small molecules and peptides that target important processes in the organisms that cause infectious diseases. This goal is being pursued via two major research directions that reflect the areas of chemistry and biology and their interface. First is the use of boronic acid-containing compounds as potential small molecule pharmaceutical agents. Second is the development of new techniques for the generation of peptide libraries and the subsequent selection of active members that disrupt specific protein-protein interactions.
Selected Scholarly Activity
Tomsho JW, Benkovic SJ. Elucidation of the mechanism of the reaction between phenylboronic acid and a model diol, Alizarin Red S. Journal of Organic Chemistry. 77(5), 2098-2106 (2012).
Tomsho JW, Pal A, Hall DG, Benkovic SJ. Ring structure and aromatic substituent effects on the pKa of the benzoxaborole pharmacophore. ACS Medicinal Chemistry Letters. 3(1), 48-52 (2012).
Baker SJ, Tomsho JW, Benkovic SJ. Boron-containing inhibitors of synthetases. Chemical Society Reviews. 40(8), 4279-4285 (2011).
An S, Deng Y, Tomsho JW, Kyoung M, Benkovic SJ. Microtubule-assisted mechanism for functional metabolic macromolecular complex formation. Proceedings of the National Academy of Sciences, 107, 12872-12876 (2010).
McGuire JJ, Bartley DM, Tomsho JW, Haile WH, Coward JK. Inhibition of human folylpolyglutamate synthetase by diastereomeric phosphinic acid mimics of the tetrahedral intermediate. Archives of Biochemistry and Biophysics. 488, 140-145 (2009).
Tomsho JW, Moran RG, Coward JK. Concentration-dependent processivity of multiple glutamate ligations catalyzed by folylpoly-g-glutamate synthetase. Biochemistry. 47, 9040-9050 (2008).
Tomsho JW, Benkovic SJ. Unnatural translation initiation. ACS Chemical Biology. 3(2), 87-88 (2008).
Cheng L, Naumann TA, Horswill AR, Hong SJ, Venters BJ, Tomsho JW, Benkovic SJ, Keiler KC. Discovery of antibacterial cyclic peptides that inhibit the ClpXP protease. Protein Science. 16(8), 1535-1542 (2007).
Tomsho JW, Coward JK. Synthesis and biological evaluation of (6S)- and (6R)-5,10-dideaza-5,6,7,8-tetrahydropteroyl poly-g-glutamates as substrates for human folylpoly-g-glutamate synthetase. Organic and Biomolecular Chemistry. 3, 3388-3398 (2005).
Davis WR, Tomsho J, Nikam S, Cook EM, Somand D, Peliska JA. Inhibition of HIV-1 reverse transcriptase-catalyzed DNA strand transfer reactions by 4-chlorophenylhydrazone of mesoxalic acid. Biochemistry. 39(46), 14279-14291 (2000).
Tomsho J, McKee J, Zanger M. A micro-scale synthesis of the diastereomers of 2,3-dibromosuccinic acid.Journal of Chemical Education. 76(1), 73-74 (1999).
Tomsho JW, Benkovic SJ. Examination of the reactivity of benzoxaboroles and related compounds with a cis-diol. Oral presentation at the 224th American Chemical Society National Meeting and Exposition, August 20, 2012.
Tomsho JW, Benkovic SJ. Elucidation of the reaction between aryl-boronic acids and a cis-diol. Poster presentation at American Chemical Society Mid-Atlantic Regional Meeting, May 21, 2011.
- American Chemical Society, since 1997
- Rho Chi, the Academic Honor Society in Pharmacy, since 2005
- Sigma Xi, the Scientific Research Society, since 2005
|Office location:||Griffith Hall, Room 300|
|Mailing address:||Department of Chemistry and Biochemistry|
University of Sciences
600 South 43rd Street
Philadelphia, PA 19104-4495
j [dot] tomsho [at] usciences [dot] edu