These findings reveal that significant modifications to Indolicidin's amino acid sequence and 3D structure do not impair its intracellular activity. Instead, these modifications highlight the peptide's broad and adaptable mechanism, as its interactions with DNA and associated biosynthetic enzymes do not rely on highly specific molecular recognition but rather involve more promiscuous interactions. Studies by , , and demonstrate how natural peptide sequences can be tailored in multiple ways to enhance one or more mechanisms of action, effectively shifting Indolicidin's activity spectrum to target specific bacterial species.