In our group, we use computational biology and synthetic biology techniques to discover, design and test new antimicrobial molecules.
We borrow from nature and harness the potential of antimicrobial peptides (AMPs). These are small proteins most all higher organisms produce that lyse and kill bacteria rapidly. AMPs have been successful during evolutionary timescales, so there is only slight chance bacteria could quickly develop resistance to them.
We use mathematical models, to explain the ways these molecules disrupt bacterial and human cells. We study the thermodynamics and kinetics that underlie the antimicrobial mechanism of action.
With detailed explanations we should have a better chance of designing antimicrobial peptides with therapeutic potential. Typically, as is well established, antimicrobial peptides bind on cell membranes, form aggregates, and disrupt the integrity of the membrane. What is not known is the set of thermodynamic and kinetic driving forces behind all the biophysical steps that underlie biological function, and what are the sequence and structural features of AMPs that render them bactericidal and toxic.
With collaborators at the Centers for Disease Control, the Mayo Clinic and the Medical School at UofMinn we are engineering new AMPs with therapeutic potential.