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Nanomolar LL-37 induces permeability of a biomimetic mitochondrial membrane
- Source :
- Nanoscale. 14(47)
- Publication Year :
- 2022
-
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.
- Subjects :
- Biomimetics
Mitochondrial Membranes
Humans
General Materials Science
Subjects
Details
- ISSN :
- 20403372
- Volume :
- 14
- Issue :
- 47
- Database :
- OpenAIRE
- Journal :
- Nanoscale
- Accession number :
- edsair.doi.dedup.....addc9f8d8866e6cd550e1a3122eae663