Fusion Peptides Enhance Bacterial Membrane Penetration and Targeting

The patent combines two distinct peptide functions into a single fusion peptide: (1) a membrane penetration domain from proline-rich antimicrobial peptides that enables cell entry, and (2) a sliding clamp binding domain that provides target-specific inhibition. This merging resolves the contradiction by integrating both membrane penetration capability and target binding affinity into one molecule, allowing the peptide to successfully deliver its therapeutic function inside bacterial cells.

The fusion peptide is segmented into distinct functional modules: an N-terminal membrane penetration domain derived from proline-rich antimicrobial peptides and a C-terminal sliding clamp binding domain with high target specificity. This segmentation allows each domain to independently perform its specialized function - the penetration domain facilitates cellular uptake while the binding domain ensures specific target engagement, thereby resolving the contradiction between uptake efficiency and target specificity.