Living cells are highly organized chemical systems in which diverse and tightly controlled reactions regulate biomolecular structure and function. Protein post-translational modifications (PTMs) arise from these reactions and introduce chemically distinct functional groups that expand protein reactivity, interaction networks, and regulatory potential. In the brain and nervous system, where molecular signaling depends on precise spatial and temporal control, even subtle alterations in protein modifications can lead to profound changes in biomolecular interactions and contribute to neurological disease.
Our research integrates biochemistry, protein chemistry, chemical biology, and neurochemistry to investigate the roles of disease-associated protein PTMs in the brain and neurons. We focus on how specific chemical transformations on proteins govern molecular recognition, enzymatic activity, and higher-order assemblies relevant to brain and neurological disorders.
To address these questions, we employ peptide and protein synthesis, protein engineering, quantitative biochemical assays, and cell-based models to establish direct causal links between PTMs and biological outcomes. By developing and applying molecular tools, we enable mechanistic interrogation of PTM-driven processes across biochemical, structural, and cellular levels. Our long-term goal is to establish a chemical framework for understanding disease-associated PTMs and to leverage this knowledge toward mechanism-based therapeutic strategies.