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Updated: Jun 28, 2026

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization
Published on: August 11, 2018
From membrane disruption to intracellular targets: A solid-state NMR perspective on antimicrobial peptide mechanism
Yijin Zhang1, Yajing Zou1, Jun Yang2
1Interdisciplinary Institute of NMR and Molecular Sciences, School of Chemistry and Chemical Engineering, The State Key Laboratory of Refractories and Metallurgy, Wuhan University of Science and Technology, Wuhan, 430081, PR China.
Abstract:
Antimicrobial peptides (AMPs) are promising alternatives to conventional antibiotics due to their broad-spectrum activity and low tendency to induce resistance. Based on their modes of action, AMPs are generally classified as membrane-active or intracellular-targeting peptides. Rational design of next-generation AMPs with enhanced efficacy and reduced cytotoxicity requires a detailed understanding of their antimicrobial mechanisms. Solid-state nuclear magnetic resonance (ssNMR) has emerged as a powerful tool for probing AMP-target interactions, providing high-resolution structural and dynamic information under native-like membrane conditions. This review summarizes recent advances in ssNMR methodologies applicable in model membranes and intact cells and highlights their contributions to elucidating AMP antimicrobial mechanisms. Representative investigations reveal that the membrane-active peptide protegrin-1 disrupts lipid bilayers via a toroidal pore mechanism, whereas lipid II-targeting AMPs inhibit cell wall biosynthesis by immobilizing lipid II through supramolecular assembly.
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