M. Clifford

Temporin B forms hetero-oligomers with Temporin L, modifies its membrane activity and increases the cooperativity of its antibacterial pharmacodynamic profile

This study shows that temporin B enhances the antibacterial cooperativity of temporin L by forming hetero-oligomers, altering membrane interaction and increasing efficacy against EMRSA-15.

Parallel evolution of frog antimicrobial peptides produces identical conformations but subtly distinct membrane and antibacterial activities

This study compares two frog antimicrobial peptides, temporin L and aurein 2.5, to understand their differing antibacterial activities despite similar structures.