Xenobiotic Binding Domain of Glutathione S-Transferase Has Cryptic Antimicrobial Peptides

Antimicrobial peptides are one of the important components of innate immune defense system and play a critical role in controlling infections. Although vast sequence and structural diversities exist, AMPs share several common features like cationicity, amphipathicity and membrane permeabilisation as mode of action. In this study, a moderately short cationic and hydrophobic peptides derived from the conserved domains of human glutathione S-transferase (GST) have been shown to have antimicrobial activity against Staphylococcus aureus ATCC 29213 and Klebsiella pneumoniae ATCC 7637 in physiological conditions without any toxicity issues. We further shown here that human GST, a C-terminal region which showed the higher antimicrobial activity, is conserved in the vertebrates. Our results demonstrate the potential of human GST derived peptides as a template for the development of anti-infective therapeutics.