期刊
MEMBRANES
卷 5, 期 4, 页码 576-596出版社
MDPI
DOI: 10.3390/membranes5040576
关键词
self-assembled monolayers; tethered bilayer lipid membranes; electrochemical impedance spectroscopy; cyclic voltammetry; large unilamellar vesicles; fluorescence; multiple sclerosis; autoantibodies; -turn peptide structures
类别
资金
- Fondazione Ente Cassa Risparmio di Firenze (Italy)
- Chaire d'Excellence of Agence Nationale de la Recherche (France) [ANR-09-CEXC-013-01]
The interaction of lipid environments with the type I' -turn peptide structure called CSF114 and its N-glucosylated form CSF114(Glc), previously developed as a synthetic antigenic probe recognizing specific autoantibodies in a subpopulation of multiple sclerosis patients' serum, was investigated by fluorescence spectroscopy and electrochemical experiments using large unilamellar vesicles, mercury supported lipid self-assembled monolayers (SAMs) and tethered bilayer lipid membranes (tBLMs). The synthetic antigenic probe N-glucosylated peptide CSF114(Glc) and its unglucosylated form interact with the polar heads of lipid SAMs of dioleoylphosphatidylcholine at nonzero transmembrane potentials, probably establishing a dual electrostatic interaction of the trimethylammonium and phosphate groups of the phosphatidylcholine polar head with the Glu(5) and His(9) residues on the opposite ends of the CSF114(Glc) -turn encompassing residues 6-9. His(9) protonation at pH 7 eliminates this dual interaction. CSF114(Glc) is adsorbed on top of SAMs of mixtures of dioleoylphosphatidylcholine with sphingomyelin, an important component of myelin, whose proteins are hypothesized to undergo an aberrant N-glucosylation triggering the autoimmune response. Incorporation of the type I' -turn peptide structure CSF114 into lipid SAMs by potential scans of electrochemical impedance spectroscopy induces defects causing a slight permeabilization toward cadmium ions. The N-glucopeptide CSF114(Glc) does not affect tBLMs to a detectable extent.
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