Brigita Urbanc, PhD, completed her studies in physics at the University of Ljubljana in Slovenia, specializing in theoretical soft condensed matter of ferroelectric liquid crystals. During her postdoctoral training at the Center for Polymer Studies at Boston University she has applied statistical physics and computational modeling to unravel the role of amyloid β-protein (Aβ) in Alzheimer’s disease. Professor Urbanc is the author of dozens of peer-reviewed papers in top-tier publications. In addition, she serves on the editorial boards of the Journal of Biological Physics and Biomolecules.
Dr. Urbanc joined the Department of Physics at Drexel University in 2008 as a member of the Biophysics Research Group. Her biophysics research revolves around conformational dynamics, folding and self-assembly of intrinsically disordered peptides and proteins, such as Aβ, as well as protein-protein and protein-lipid interactions of relevance to human diseases. Her group is applying multi-scale molecular dynamics approaches and in vitro approaches, including chemical cross-linking, gel electrophoresis, and fluorescence spectroscopy. Her group also pursues the assessment and development of the molecular dynamics force field for intrinsically disordered peptides. The research of her group has been supported by National Institutes of Health and the National Science Foundation.
Professor Urbanc strives to support and promote women and underrepresented minorities in STEM fields. She has been the academic advisor to the undergraduate student organization Women in Physics Society since its formation in 2011 and has served as the associate head for graduate studies in the Department of Physics since 2020.
She has mentored 14 undergraduate students, 16 graduate or visiting students –seven of whom successfully defended their master’s or PhD theses– and three postdoctoral fellows. She believes that a multidisciplinary collaborative approach is the most effective way to further advances in science and tackle complex problems, such as Alzheimer’s disease, the leading cause of dementia in the elderly worldwide.
B. Andrews, J. Guerra, R. Schweitzer-Stenner, and B. Urbanc (2022) Do Molecular Dynamics Force Fields Accurately Model Ramachandran Distributions of Amino Acid Residues in Water?, Phys. Chem. Chem. Phys. 22, 3259-3279.
B. Urbanc (2021) Cross-Linked Amyloid β-Protein Oligomers: A Missing Link in Alzheimer's Disease Pathology?, invited perspective, J. Phys. Chem. B 125, 1307-1316.
B. Andrews, S. Zhang, R. Schweitzer-Stenner, and B. Urbanc (2020) Glycine in Water Favors the Polyproline II State, Biomolecules 10, 1121.
S. Zhang, R. Schweitzer-Stenner, and B. Urbanc (2020) Do Molecular Dynamics Force Fields Capture Conformational Dynamics of Alanine in Water? J. Chem. Theor. Comput. 16, 510-527; J. Chem. Theor. Comput. 16, 5982.
M. J. Voelker, B. Barz, and B. Urbanc (2017) Fully-Atomistic Aβ40 and Aβ42 Oligomers in Water: Observation of Pore-Like Conformations, J. Chem. Theor. Comput. 13, 4567-4583. Features cover art at http://pubs.acs.org/toc/jctcce/13/9
M. T. Mawhinney, T. L. Williams, J. L. Hart, M. L. Taheri, and B. Urbanc (2017) Elucidation of Insulin Assembly in Acidic and Neutral pH: Characterization of Low Molecular Weight Oligomers, Proteins: Structure, Functions, and Bioinformatics, 85, 2096-2110.
T.L. Williams, L.C. Serpell, and B. Urbanc (2016) Stabilization of Native Amyloid β-Protein Oligomers by Copper and Hydrogen Peroxide Induced Cross-Linking of Unmodified Proteins (CHICUP), Biochim. Biophys. Acta 1864, 249-259 .
B. Barz and B. Urbanc (2014) Minimal Model of Self-Assembly: Emergence of Diversity and Complexity, J. Phys. Chem. B 118, 3761-3770 (2014). Features cover art at https://pubs.acs.org/toc/jpcbfk/118/14
B. Barz and B. Urbanc (2012) Dimer Formation Enhances Structural Differences between Amyloid β-Protein (1-40) and (1-42): An Explicit-Solvent Molecular Dynamics Study, PLoS ONE 7, e34345.
B. Urbanc, M. Betnel, L. Cruz, G. Bitan, and D.B. Teplow (2010) Elucidation of amyloid β-protein oligomerization mechanisms: Discrete molecular dynamics study, J. Am. Chem. Soc. 132, 4266-4280.