[4] Like the antimicrobial peptides pyrrhocoricin and abaecin, drosocin early studies showed it can bind to bacterial DnaK, inhibiting cell machinery and replication.

[5][6] However the action of these drosocin-like peptides may instead be to bind to microbe ribosomes, preventing protein translation.

[9] In the absence of pore-forming peptides, the related AMP pyrrhocoricin is taken into the bacteria by the action of uptake permeases.

[13] The bolded threonine residue acts as a site for O-glycosylation, also found in the AMPs abaecin and pyrrhocoricin.

The underlined PRP motifs are key to the binding of such peptides to the DnaK proteins of bacteria.