Structural Characteristics of Glycocins: Unraveling the Role of S-Linked Carbohydrates and Other Structural Elements

Glycocins are antimicrobial peptides with glyco-sylations, often an S-linked monosaccharide. Their recent structure elucidation has brought forth questions about their mechanisms of action as well as the impact of S-glycosylation on their structural behavior. Here, we investigated structural characteristics of glycocins using a computational approach. Depending on the peptide's class (sublancin-or glycocin F-like), the sugar changes the peptide's flexibility. Also, the presence of glycosylation is necessary for the lack of structure of Asm1. The C-terminal tail in glycocin F-like peptides influenced their structured regions, acting like a regulator. These findings corroborate the versatility of these post-translational modifications, pointing toward their potential use in molecular engineering.

Automated summary

This study investigated the structural characteristics of glycocins using a computational approach and found that glycosylation can affect the flexibility and structural behavior of peptides. Specifically, the C-terminal tail in glycocin F-like peptides serves as a regulator for their structured regions, indicating the versatility of glycocins and their potential use in molecular engineering.