Lydia was born and raised in the Cleveland area. She received her Bachelor of Science degree from Wittenberg University in 2010. During undergrad, she participated in research at Clemson University and at the University of Colorado at Boulder. Lydia then left the great state of Ohio for Houston, Texas, where she was a NSF graduate research fellow at Rice University under Prof. Christy Landes. She received her Doctor of Philosophy in Chemistry in 2015.
In the BioInterfaces and Cell Mechanics Group, Lydia is a Beckman-Brown interdisciplinary postdoctoral fellow collaborating with the groups of Prof. Martin Gruebele and Prof. Paul Braun to investigate protein folding dynamics in different interfacial (lipid, polymer, hydrogel) environments using fluorescent techniques.
More information can be found at Lydia's personal site.
Research Project Summary: The powerful capabilities of proteins have inspired their use at abiotic, material surfaces for diverse applications as biosensors, biologic pharmaceuticals, tissue engineering scaffolds, and drug targets. When proteins interact with materials, their structure and conformational dynamics, and hence function, can be altered compared to those in solution and in vivo. But determining how surface materials alter protein folding stability in situ is difficult with current, mostly noninterfacial techniques.
I am developing a novel fluorescence microscopy approach to understand the design rules of materials that enhance protein folding stability and function. The technique, Fast Relaxation Imaging (FReI), has been used previously in cells, but currently has untapped potential to study biomaterials. FReI uses proteins labeled with a fluorescence resonance energy transfer (FRET) pair, where a donor dye transfers energy to the acceptor dye. The ratio of donor/acceptor fluorescence (D/A) is sensitive to nanoscale changes in distance. In FReI, a temperature jump is applied and by monitoring D/A before, during, and after the jump, the initial state, unfolding, and refolding of the protein can be spatiotemporally monitored.
I have extended the FReI approach to studies of protein folding in hydrogels, showing that the polymer chemistry of the hydrogel influences the protein dynamics more than the confinement effects of the nanopores within the hydrogel. The hydrogel polymer causes an increase in protein stability, speeds up folding relaxation, and promotes irreversible binding of the protein to the polymer. The ACS Applied Materials and Interfaces manuscript can found here. In future work, I am extended the FReI approach to studies of protein folding on polymer brush and gradient materials that enable methodological measurement of a “library” of diverse surface compositions on a single substrate.