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Interaction Study of Phospholipid Membranes with an N-Glucosylated β-Turn Peptide Structure Detecting Autoantibodies Biomarkers of Multiple Sclerosis

1
Department of Chemistry "Ugo Schiff", University of Florence, Via della Lastruccia 13, 50019 Sesto Fiorentino, Italy
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Interdepartmental Laboratory of Peptide and Protein Chemistry and Biology, Via della Lastruccia 13, 50019 Sesto Fiorentino, Italy
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Department of Chemical Sciences and Technologies, University of Rome 'Tor Vergata', Via Ricerca Scientifica 1, 00133 Rome, Italy
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Department of Neurosciences, Psychology, Drug Research and Child Health—Section of Pharmaceutical Sciences and Nutraceutics, University of Florence, Via Ugo Schiff 6, 50019 Sesto Fiorentino, Italy
5
[email protected] Platform and Laboratory of Chemical Biology EA4505, University of Cergy-Pontoise, 5 mail Gay-Lussac, 95031 Cergy-Pontoise CEDEX, France
6
Department of Chemistry, University of Padova, Via Marzolo 1, 35131 Padova, Italy
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Shiro Suetsugu
Membranes 2015, 5(4), 576-596; https://doi.org/10.3390/membranes5040576
Received: 27 June 2015 / Accepted: 24 September 2015 / Published: 30 September 2015
The interaction of lipid environments with the type I’ β-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 Glu5 and His9 residues on the opposite ends of the CSF114(Glc) β-turn encompassing residues 6-9. His9 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’ β-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. View Full-Text
Keywords: self-assembled monolayers; tethered bilayer lipid membranes; electrochemical impedance spectroscopy; cyclic voltammetry; large unilamellar vesicles; fluorescence; multiple sclerosis; autoantibodies; β-turn peptide structures self-assembled monolayers; tethered bilayer lipid membranes; electrochemical impedance spectroscopy; cyclic voltammetry; large unilamellar vesicles; fluorescence; multiple sclerosis; autoantibodies; β-turn peptide structures
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Becucci, L.; Benci, S.; Nuti, F.; Real-Fernandez, F.; Vaezi, Z.; Stella, L.; Venanzi, M.; Rovero, P.; Papini, A.M. Interaction Study of Phospholipid Membranes with an N-Glucosylated β-Turn Peptide Structure Detecting Autoantibodies Biomarkers of Multiple Sclerosis. Membranes 2015, 5, 576-596.

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