Issue 47, 2022

Nanomolar LL-37 induces permeability of a biomimetic mitochondrial membrane

Abstract

LL-37, the only human host cathelicidin peptide, is proposed to be able to induce host cell apoptosis through mitochondrial membrane permeabilization (MMP). Detailed pathways of the LL-37-triggered MMP are however still disputed. It is generally believed that cationic peptides permeate a membrane mostly in conditions of micromolar peptide concentrations and negatively charged membranes, which are not usually satisfied in the mitochondrial circumstance. Herein, using a variety of single-molecule techniques, we show that nanomolar LL-37 specifically induces permeability of a phosphoethanolamine (PE)-rich biomimetic mitochondrial membrane in a protein-independent manner. The insertion dynamics of single LL-37 molecules exhibit different metastable states in bilayers composed of different lipids. Moreover, the PE lipids significantly facilitate adsorption and accumulation of LL-37 on the PE-rich bilayer, and produce deeper insertion of peptide oligomers, especially tetramers, into the bilayer. This work offers an alternative pathway of the LL-37-triggered MMP and apoptosis.

Graphical abstract: Nanomolar LL-37 induces permeability of a biomimetic mitochondrial membrane

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Article information

Article type
Paper
Submitted
30 সেপ্টে. 2022
Accepted
15 নভে. 2022
First published
16 নভে. 2022

Nanoscale, 2022,14, 17654-17660

Nanomolar LL-37 induces permeability of a biomimetic mitochondrial membrane

X. Jiang, C. Yang, J. Qiu, D. Ma, C. Xu, S. Hu, W. Han, B. Yuan and Y. Lu, Nanoscale, 2022, 14, 17654 DOI: 10.1039/D2NR05409D

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