Báo cáo Y học: Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity

Thermolysin-Linearized Microcin J25 Retains the Structured Core of the Native Macrocyclic Peptide and Displays Antimicrobial Activity

Tác giả: Alain Blond, Michel Cheminant, Delphine Destoumieux-Garzón, Isabelle Ségalas-Milazzo, Jean Peduzzi, Christophe Goulard, and Sylvie Rebuffat

Lĩnh vực: Biochemistry, Microbiology

Nội dung tài liệu: This study investigates the structure and antimicrobial activity of thermolysin-linearized microcin J25 (MccJ25-L1-21), a macrocyclic antimicrobial peptide. The research aimed to understand the molecular mechanisms behind MccJ25’s biosynthesis, folding, and mode of action. The study reveals that MccJ25-L1-21 retains a structured core similar to the native cyclic peptide and exhibits significant antibacterial activity against *Salmonella* and *Escherichia* strains. The findings highlight the importance of the 8-19 region and the Gly11-His16 loop for moderate antibacterial activity, while the Phe21-Pro6 loop and the macrocyclic backbone are crucial for complete activity. The research also demonstrates the remarkable stability of the structured core in MccJ25-L1-21 under harsh conditions.

Mục lục chi tiết:

• Introduction
• Materials and Methods
• Results
• Discussion
• Acknowledgements
• References
• Supplementary Material