Selectivity of Antimicrobial Peptides: A Complex Interplay of Multiple Equilibria

摘要: Antimicrobial peptides (AMPs) attack bacterial membranes selectively, killing microbes at concentrations that cause no toxicity to the host cells. This selectivity is not due interaction with specific receptors but determined by different lipid compositions of two cell types and peculiar physicochemical properties AMPs, particularly their cationic amphipathic character. However, available data, including recent studies peptide-cell association, indicate this picture excessively simplistic, because modulated a complex interplay several interconnected phenomena. For instance, conformational transitions self-assembly equilibria modulate effective peptide hydrophobicity, electrostatic hydrophobic contributions membrane-binding driving force are nonadditive, kinetic processes can play an important role in selective presence All these phenomena bearing on final activity AMPs must be considered definition design principles optimize selectivity.