Professor David Sholl
“Using High Throughput Computation to Accelerate
Development of Materials for Scalable Energy Technologies”
Computational modeling of materials can be a powerful complement to experimental methods when models with useful levels of predictive ability can be deployed more rapidly than experiments. Achieving this goal involves judicious choices about the level of modeling that is used and the key physical properties of the materials of interest that control performance in practical applications. I will discuss two examples of using high throughput computations to identify new materials for scalable energy applications: the use of metalorganic frameworks in membranes and gas storage and the selection of metal hydrides for high temperature nuclear applications. These examples highlight the challenges of generating sufficiently comprehensive material libraries and the potential advantages and difficulties of using computational methods to examine large libraries of materials.
Wednesday, October 14, 2015
12:30 pm, HED Room 116
Professor Amy Karlsson
Department of Chemical and Biomolecular Engineering
University of Maryland
“Engineering Peptides and Proteins to Combat Human Disease”
Rational design and directed evolution are both powerful approaches for engineering proteins and peptides. Our lab applies these approaches to exploit the power of proteins and peptides in studying and combatting human disease, and I will discuss applications of protein engineering in fungal disease and cancer. We applied a rational design approach to engineer non-natural antimicrobial β-peptides that exhibit antifungal activity against the fungal pathogen Candida albicans. Through this work, we developed a deeper understanding of the properties of β-peptides that contribute to their toxicity towards fungal cells and fungal biofilms, and we are currently working on ways to apply this understanding to designing improved antifungal agents. We have also used directed evolution to engineer antibodies that can fold and function inside cells, which has broad applications in human diseases, including cancer. The reducing environment inside cells prevents formation of the disulfide bonds normally required for proper antibody folding, but we have developed a bacterial inner membrane display system that harnesses the cytoplasmic folding quality control mechanisms of the Escherichia coli twin-arginine translocation pathway to engineer proteins able to fold in the cytoplasmic environment. We used this method to display and screen a combinatorial library of single-chain variable fragment (scFv) antibodies and isolated scFvs with dramatic improvements in both antigen-binding and intracellular solubility. We are now using our display method to engineer scFvs for studying and treating cancer and fungal disease.
Dr. Amy J. Karlsson received her bachelor’s degree in chemical engineering from Iowa State University in 2003 and then joined Prof. Sean Palecek’s group at the University of Wisconsin, where she received her PhD in chemical engineering in 2009. Following her doctoral work, she was an NIH Ruth L. Kirschstein Postdoctoral Fellow in Prof. Matt DeLisa’s lab at Cornell University. Dr. Karlsson joined the Department of Chemical and Biomolecular Engineering at the University of Maryland as an assistant professor in 2012. Her group’s research lies at the interface of biology and engineering and uses protein engineering strategies to improve the understanding of human diseases and develop tools for drug design and disease diagnosis.
Thursday, May 1, 2014
12:45 pm, ZHS Room 159
The scientific community is cordially invited.