Molecular design drives nanoarchitecture in self-assembling antimicrobial peptides

Antimicrobial peptides (AMPs) have emerged as promising alternatives owing to their broad-spectrum activity and reduced potential for resistance. Recent advances have highlighted the role of peptide self-assembly in enhancing the stability, bioavailability, and efficacy of AMPs. Through non-covalent interactions, self-assembly enables the formation of nanostructures, including nanofibers, nanotubes, and micelles. This process can enhance antimicrobial activity by increasing AMP stability, facilitating membrane interactions, and modulating the mechanisms of bacterial disruption. Physicochemical features, including hydrophobicity, charge distribution, and aromatic interactions, allow the creation of tailored nanostructures with enhanced antimicrobial performance. Furthermore, self-assembled AMPs offer controlled drug release, targeted delivery, and synergistic strategies. This review examines the molecular mechanisms underlying peptide self-assembly and highlights their influence on AMP functionality and potential applications in combating infections.