Discussions

Amphipathic structures in α-helical and β-sheet peptides contribute significantly to their biological activity by facilitating interactions with diverse biological environments. In such structures, one side of the peptide displays polar, hydrophilic side chains, while the opposite side features nonpolar, hydrophobic side chains. This dual-characteristic allows amphipathic peptides to engage effectively with cell membranes, proteins, and other biomolecules, influencing processes such as cell signaling, antimicrobial activity, and protein-protein interactions. The spatial arrangement enhances the ability of the peptide to anchor into lipid bilayers or interface with other hydrophobic or hydrophilic regions within the biological milieu, making these structures critical to the peptide’s function and efficacy.