By examining the mechanism of membrane permeation in a range of molecules that control membrane topology, including antimicrobial peptides, cell penetrating peptides, and viral fusion peptides, we show how a combination of geometry, coordination chemistry, and soft matter physics can be used to approach a unified understanding of the amino acid sequence requirements of membrane permeation. Using these ideas, we demonstrate that it is possible to renovate old antibiotics by adding new functions. In a parallel line of inquiry, we will also show how the multi-functionality of antimicrobial peptides can lead to auto-immune diseases such as lupus and psoriasis.

Teaching old antibiotics new tricks

248th National Meeting (2014)

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