Melittin adsorption and lipid monolayer disruption at liquid-liquid interfaces

Langmuir. 2011 Nov 15;27(22):13918-24. doi: 10.1021/la202970g. Epub 2011 Oct 19.

Abstract

Melittin, a membrane-active peptide with antimicrobial activity, was investigated at the interface formed between two immiscible electrolyte solutions (ITIES) supported on a metallic electrode. Ion-transfer voltammetry showed well-defined semi-reversible transfer peaks along with adsorptive peaks. The reversible adsorption of melittin at the liquid-liquid interface is qualitatively discussed from voltammetric data and experimentally confirmed by real-time image analysis of video snapshots. It is also demonstrated that polarization of the water/1,2-DCE interface results in drastic drop shape variations caused by large variations of the interfacial tension. The experimental data also confirmed that maximum adsorption occurs near the ion transfer potential. Finally, the interaction of melittin with a monolayer of L-α-dipalmitoyl phosphatidylcholine (DPPC) was also investigated showing that melittin destabilizes the lipidic monolayer facilitating its desorption. The non-covalent complex formation between melittin and DPPC was confirmed by mass spectrometry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1,2-Dipalmitoylphosphatidylcholine / chemistry*
  • Adsorption
  • Melitten / chemistry*
  • Spectrometry, Fluorescence
  • Spectrometry, Mass, Electrospray Ionization
  • Spectrophotometry, Ultraviolet

Substances

  • Melitten
  • 1,2-Dipalmitoylphosphatidylcholine