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In recent years, peptide self-assembly proved to be an efficient strategy to create complex structures or functional materials with nanoscale precision. In this work, we designed and synthesized a novel glycopeptide molecule with a galactose moiety through peptide galactosylation. Then relying on peptide self-assembling strategies, we created a supramolecular hydrogel with multivalent galactose ligands on the surface of self-assembled nanofibers for molecular recognition and interactions. Because of multivalent galactose–LecA interactions, the self-assemblies of glycopeptide could target P. aeruginosa specifically, and acted as anti-virulence and antibacterial agents to inhibit biofilm formation and bacterial growth of P. aeruginosa. Moreover, in association with polymyxin B, a common antibiotic, the glycopeptide hydrogel exhibited a synergistic growth inhibition effect on biofilm colonization of P. aeruginosa.

In recent years, peptide self-assembly proved to be an efficient strategy to create complex structures or functional materials with nanoscale precision. In this work, we designed and synthesized a novel glycopeptide molecule with a galactose moiety through peptide galactosylation. Then relying on peptide self-assembling strategies, we created a supramolecular hydrogel with multivalent galactose ligands on the surface of self-assembled nanofibers for molecular recognition and interactions. Because of multivalent galactose-LecA interactions, the self-assemblies of glycopeptide could target