Mechanistic insights from dynamic structural changes of model bacterial cytoplasmic membranes challenged by Gemini surfactant octenidine

Octenidine dihydrochloride (OCT) is a Gemini surfactant that is highly potent in bacterial membrane disruptions via a multitude of molecular interactions mediated by its cationic 4-aminopyridinium headgroup and hydrophobic tail and spacer groups. However, the mechanistic details for such interactions remain to be fully understood. Here, structural changes of unilamellar ternary liposomes comprising 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine (DPPE), 1,2-dipalmitoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (DPPG) and cardiolipin (CL), mimicking the cytoplasmic membrane of E. coli bacteria, challenged by OCT at different lipid:surfactant molar ratios (50:1-1:1) and different temperatures (25, 40, and 70 °C), have been studied using synchrotron time-resolved stopped flow small-angle X-ray scattering (TR-SAXS), complemented by wide-angle X-ray scattering (WAXS), dynamic light scattering and zeta potential measurements. The high temporal resolution of the scattering data offered insights into the breakdown-reassembly mechanism of liposome disruption, involving initial membrane lysing and subsequent lipid re-assembly into multilamellar stacks, which then collapsed into a condensed multilamellar L<sub>α</sub><sup>C</sup> phase and a cubic Pn3m phase upon heating. Critical comparisons between OCT and Alkyl 8-10-8, a structurally analogous Gemini surfactant differing only with its quaternary ammonium headgroups, revealed further mechanistic insights from subtle differences in the lipid-surfactant structures. Compared to Alkyl 8-10-8, OCT mediated membrane disruption at a lower concentration, perturbing the membrane thickness and altering the membrane gel-to-fluid phase transition temperature, also causing membrane surface charge neutralisation and reversal. These findings shed light on molecular mechanism of OCT-membrane interactions and the role of the OCT headgroup architecture in its antimicrobial efficacy.

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Journal
Journal of Colloid and Interface Science
Published
2026-03-09
DOI
https://doi.org/10.1016/j.jcis.2026.140260
Primary Topic
Lipid Membrane Structure and Behavior
Type
article
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article

Mechanistic insights from dynamic structural changes of model bacterial cytoplasmic membranes challenged by Gemini surfactant octenidine

Lauren Matthews, Magdalena Wlodek, Wuge H. Briscoe, Rebecca J. Fong et al.
Journal of Colloid and Interface Science
Lipid Membrane Structure and Behavior
article

Mechanistic insights from dynamic structural changes of model bacterial cytoplasmic membranes challenged by Gemini surfactant octenidine

Lauren Matthews, Magdalena Wlodek, Wuge H. Briscoe, Rebecca J. Fong, Eva M. Perez-Prat, Charlotte Kenton, Oliver J. McDowell, Najet Mahmoudi, Egor A. Bersenev
article en

Abstract

Octenidine dihydrochloride (OCT) is a Gemini surfactant that is highly potent in bacterial membrane disruptions via a multitude of molecular interactions mediated by its cationic 4-aminopyridinium headgroup and hydrophobic tail and spacer groups. However, the mechanistic details for such interactions remain to be fully understood. Here, structural changes of unilamellar ternary liposomes comprising 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine (DPPE), 1,2-dipalmitoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (DPPG) and cardiolipin (CL), mimicking the cytoplasmic membrane of E. coli bacteria, challenged by OCT at different lipid:surfactant molar ratios (50:1-1:1) and different temperatures (25, 40, and 70 °C), have been studied using synchrotron time-resolved stopped flow small-angle X-ray scattering (TR-SAXS), complemented by wide-angle X-ray scattering (WAXS), dynamic light scattering and zeta potential measurements. The high temporal resolution of the scattering data offered insights into the breakdown-reassembly mechanism of liposome disruption, involving initial membrane lysing and subsequent lipid re-assembly into multilamellar stacks, which then collapsed into a condensed multilamellar L<sub>α</sub><sup>C</sup> phase and a cubic Pn3m phase upon heating. Critical comparisons between OCT and Alkyl 8-10-8, a structurally analogous Gemini surfactant differing only with its quaternary ammonium headgroups, revealed further mechanistic insights from subtle differences in the lipid-surfactant structures. Compared to Alkyl 8-10-8, OCT mediated membrane disruption at a lower concentration, perturbing the membrane thickness and altering the membrane gel-to-fluid phase transition temperature, also causing membrane surface charge neutralisation and reversal. These findings shed light on molecular mechanism of OCT-membrane interactions and the role of the OCT headgroup architecture in its antimicrobial efficacy.

Journal of Colloid and Interface ScienceVol. 715
DSM (Netherlands) (NL), Rutherford Appleton Laboratory (GB), European Synchrotron Radiation Facility (FR), University of Bristol (GB), Procter & Gamble (United Kingdom) (GB)
Openalex Percentile: Top 28%
Lipid Membrane Structure and Behavior
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