Juszczak, Laura J.
Associate professor, Chemistry, Brooklyn College and The Graduate Center
Associate professor, Biochemistry, The Graduate Center at The City University of New York
Visiting associate, Physiology and Biophysics, Albert Einstein College of Medicine
AB, Art History, Wellesley College;
MS, Art Conservation, The University of Delaware
PhD, Chemistry, New York University
PostDoc, Physiology and Biophysics, Albert Einstein College of Medicine
Several aromatic dipeptides inhibit the angiogenic proliferative effect of the angiotensin I converting enzyme, ACE I, and thus curtail malignant cell proliferation. We have shown that cation-pi (aromatic) noncovalent interactions involve charge transfer, and therefore can be studied by visible absorption and fluorescence spectroscopy. Coupled with the molecular level detail provided by in silico docking studies and molecular dynamics simulations, key noncovalent interactions are revealed, assisting in the development of optimal ACE I inhibitors.
- Laura J. Juszczak and Azaria S. Eisenberg. The Color of Cation-pi Interactions: Subtleties of Amine-Tryptophan Interaction Energetics Allow for Radical-like Visible Absorbance and Fluorescence. J Am Chem Soc. (2017) 2178302-8311, PubMed #28537725, PMC28537725
- S. Eisenberg, M. Nathan, and L. J. Juszczak. Excited State Electron Distribution and Role of the Terminal Amine in Acidic and Basic Tryptophan Dipeptide Fluorescence. J Mol Struct (2016) 111856-67, PMC4852485.
- S. Eisenberg and L. J. Juszczak. The Broken Ring: Reduced Aromaticity in Lys-Trp Cations and High pH Tautomer Correlates with Lower Quantum Yield and Shorter Lifetimes. J Phys Chem B (2014)1187059-69, PPMC4165537.
Grants over the last 5 years
- 7/13 –12/17. NIHSC3 GM105562, “Edge-on/face-on: Tryptophan tripeptides model residue interactions in proteins”