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Updated: Jan 22, 2026

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
O-Mannosylation Affords a Glycopeptide Hydrogel with Inherent Antibacterial Activities against E. coli via
Jing Li1, Shufeng Liang2,3, Yufei Yan4
1Department of Polymer Science and Engineering, College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou, 215123, China.
Abstract:
Multivalent carbohydrate-lectin interactions play a crucial role in bacterial infection. Biomimicry of multivalent glycosystems represents a major strategy in the repression of bacterial growth. In this study, a new kind of glycopeptide (Naphthyl-Phe-Phe-Ser-Tyr, NMY) scaffold with mannose modification is designed and synthesized, which is able to perform supramolecular self-assembly with the assistance of catalytic enzyme, and present multiple mannose ligands on its self-assembled structure to target mannose-binding proteins. Relying on multivalent carbohydrate-lectin interactions, the glycopeptide hydrogel is able to bind Escherichia coli (E. coli) in high specificity, and result in bacterial adhesion, membrane disruption and subsequent cell death. In vivo wound healing assays reveal that this glycopeptide hydrogel exhibits considerable potentials for promoting wound healing and preventing E. coli infection in a full-thickness skin defect mouse model. Therefore, through a specific mannose-lectin interaction, a biocompatible hydrogel with inherent antibacterial activity against E. coli is achieved without the need to resort to antibiotic or antimicrobial agent treatment, highlighting the potential role of sugar-coated nanomaterials in wound healing and control of bacterial pathogenesis.
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