Peptides that self-assemble into pore-like structures in lipid bilayers could have utility in a variety of biotechnological and clinical applications due to their ability to breach the barrier imposed by lipid bilayers. To empower such discoveries, we use rationally designed peptide libraries and high-throughput screens to select peptides based on a particular property, in this case macromolecular-size bilayer poration. Towards this goal, we have identified the PhD peptides, which efficiently assemble into large pore-like structures when triggered by low pH.  Subsequent biophysical characterization has revealed that the activity of these peptides is extremely sensitive to the composition of the lipid bilayer. Currently we are working to understand the principles of peptide-lipid interactions that underlie the observed exquisite sensitivity.

Exquisite sensitivity of PhD peptide activity to bilayer lipid composition

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.