Antimicrobial peptides (AMPs) have emerged as a promising category of antimicrobial agents, garnering considerable attention due to their wide-ranging effectiveness, limited potential for resistance development, and applicability in various clinical and industrial contexts. Nevertheless, the development of new AMPs that exhibit improved efficacy, selectivity, and stability presents a significant challenge. A viable strategy for designing more potent AMPs involves conducting structure-function analysis, which entails investigating the correlation between the structural attributes of AMPs and their biological activity. This analysis yields valuable insights into the crucial elements of AMPs that contribute to their antimicrobial action, including their primary, secondary, and tertiary structures, as well as their physicochemical properties. In our research, we introduce an innovative approach to designing novel antimicrobial peptides belonging to the Class II lantibiotic category, with a particular focus on achieving high antimicrobial activity against Bacillus thuringiensis and Listeria monocytogenes. Our findings indicate that this AMP functions by forming complexes with lipid II. To summarize, structure-function analysis represents a powerful tool in the quest to design AMPs with enhanced antimicrobial properties. This approach enables a deeper understanding of the molecular mechanisms underlying AMPs and facilitates the optimization of their structural and physicochemical characteristics for specific applications.

Awatef Ouertani earned her PhD in 2019 from the Faculty of Science at Tunis, Tunisia. Currently, she holds a postdoctoral position at the Laboratory of Biotechnology and Bio-Geo Resources Valorization, located at Biotechpole Sidi Thabet, Tunisia. As a distinguished biochemist and researcher, she has made significant contributions in the field of protein biochemistry. Her research efforts have yielded numerous notable publications that have not only reinforced her expertise but also enriched the scientific community's comprehension of protein structures, interactions, and enzymatic functions.