John S. Albin

This study identifies residues critical for separating antimicrobial activity from membrane disruption in LL-37 by modulating its dimerization interface.

This study shows that helicity and membrane permeabilization are not universal requirements for cathelicidin-mediated killing of gram-negative bacteria, and identifies lead compounds with improved selectivity.

The paper demonstrates that adding an N-terminal biphenyl motif from LL-37 to short cathelicidin peptides significantly enhances their antibacterial activity against gram-negative bacteria.

The paper identifies LL-37 variants that kill gram-negative bacteria without membrane disruption and bacteria that are permeabilized without being killed, suggesting alternative mechanisms of antibacterial activity.