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Updated: Jan 8, 2026

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Published on: November 16, 2016

細菌誘発オリゴペプチド集合による低細胞毒性および低溶血性での効果的な細菌殺傷

Yi Cheng¹, He Zhao¹, Jiayi Sun¹

¹State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Qianjin Avenue 2699, Changchun 130012, China.

Biomacromolecules

|December 24, 2025

Abstract:

Bacteria-induced on-membrane assembly of oligopeptides showed the potential for balancing their persistent conflict between antibacterial activity and biocompatibility. However, molecular determinants linking the peptide sequence, assembly behavior, antibacterial efficacy, and biocompatibility remain insufficiently understood. Here, we investigated a series of heptapeptides, (RX)₃R (X = A, I, F), and demonstrated the significant influence of hydrophobic residues on bacteria-induced assembly, antibacterial performance, cytotoxicity, and hemolytic activity. Negatively charged liposomes or bacterial membranes could induce the assembly of (RI)₃R and (RF)₃R into nanofibers, which in turn exhibited enhanced antibacterial efficacy against Gram-negative Escherichia coli with minimum inhibitory concentrations (MICs) of 60 μM but poor antibacterial activity on Gram-positive Staphylococcus aureus (MICs: 400-500 μM). Importantly, both peptides demonstrated excellent biocompatibility, with cytotoxicity thresholds of 600 μM (RI)₃R and 2000 μM (RF)₃R and hemolysis thresholds up to 2000 and 4000 μM, respectively. These findings provide valuable insights for the rational design of antibacterial oligopeptides.

キーワード:

抗菌ペプチドオリゴペプチド細菌誘発集合生体適合性ドラッグデザイン

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