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Membranes 2015, 5(4), 576-596; doi:10.3390/membranes5040576

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
2
Interdepartmental Laboratory of Peptide and Protein Chemistry and Biology, Via della Lastruccia 13, 50019 Sesto Fiorentino, Italy
3
Department of Chemical Sciences and Technologies, University of Rome 'Tor Vergata', Via Ricerca Scientifica 1, 00133 Rome, Italy
4
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
PeptLab@UCP 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
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Shiro Suetsugu
Received: 27 June 2015 / Accepted: 24 September 2015 / Published: 30 September 2015
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Abstract

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
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

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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