Functional and Structural Characterization of Drosocin and its Derivatives Linked O-GalNAc at Thr11 Residue

Antimicrobial peptides have recently gained the much attention because of their ability to make defense system from attacking bacterial infections. Drosocin has been considered as very attractive antibiotic agents because of low toxicity against human erythrocytes and active at the low concentration. We have studied the structure-activity relationship of a glycopeptide drosocin focused on the N-acetyl-D-galactoside at Thr(11) residue. Based on the radial diffusion assay, we found that the acetylation of carbohydrate moiety increased the antimicrobial activity and the Pro(10), present in the middle of drosocin plays an important role in the antimicrobial activity. Our results provide a good lead compound for further studies on the design of drosocin-based analogues targeting glyco linked Thr site.