期刊
JOURNAL OF CHEMICAL INFORMATION AND MODELING
卷 62, 期 4, 页码 927-935出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jcim.1c01001
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- CAPES
- CNPq
- FAPERGS
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.
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.
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