Secondary Study Conducted To Identify 3-Bromopyruvate Protein-Targets

Bioorthogonal Profiling of a Cancer Cell Proteome Identifies a Large Set of 3‑Bromopyruvate Targets beyond Glycolysis

Authors: Narek Darabedian¹, Thomas C. Chen², Henrik Molina³, Matthew R. Pratt¹, Axel H. Schönthal, PhD³, and Axel H. Schönthal²

In its initial study on the effects of 3-Bromopyruvate (3BP) in conjunction with Peryllil Alcohol to impact tumor cell growth by inhibiting glyceraldehyde 3-phosphate dehydrogenase (GAPDH) production resulting in energy depletion in the tumor cell, NeOnc Technologies was able to demonstrate that it’s NEO 218 formulation had a significantly higher impact on lowering GAPDH production. The study also showed that 3BP was also creating an addition of excess pyruvate, the final product of glycolysis, indicating that GAPDH may not be the only relevant target of 3BP and that modification of cysteine residues may be occurring in many different proteins.

This secondary study was conducted to directly test this hypothesis in order to determine what additional target proteins may be targeted by 3BP. Identification of these other targets will lead to a better understanding of 3BP’s ability to slow tumor cell growth, and to help eliminate any adverse secondary issues relating to this treatment protocol.

¹ Departments of Chemistry and Biological Sciences, University of Southern California, Los Angeles, California 90089, United States, ² Departments of Neurosurgery and ⊥Molecular Microbiology & Immunology, Keck School of Medicine, University of Southern California, Los Angeles, California 90089, United States, ³ Proteomics Resource Center, Rockefeller University, New York, New York 10065, United States