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Interaction Study of Phospholipid Membranes with an N-Glucosylated β-Turn Peptide Structure Detecting Autoantibodies Biomarkers of Multiple Sclerosis
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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4704000/ https://www.ncbi.nlm.nih.gov/pubmed/26437433 http://dx.doi.org/10.3390/membranes5040576 |
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author | Becucci, Lucia Benci, Stefano Nuti, Francesca Real-Fernandez, Feliciana Vaezi, Zahra Stella, Lorenzo Venanzi, Mariano Rovero, Paolo Papini, Anna Maria |
author_facet | Becucci, Lucia Benci, Stefano Nuti, Francesca Real-Fernandez, Feliciana Vaezi, Zahra Stella, Lorenzo Venanzi, Mariano Rovero, Paolo Papini, Anna Maria |
author_sort | Becucci, Lucia |
collection | PubMed |
description | 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 Glu(5) and His(9) residues on the opposite ends of the CSF114(Glc) β-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’ 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. |
format | Online Article Text |
id | pubmed-4704000 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-47040002016-01-21 Interaction Study of Phospholipid Membranes with an N-Glucosylated β-Turn Peptide Structure Detecting Autoantibodies Biomarkers of Multiple Sclerosis Becucci, Lucia Benci, Stefano Nuti, Francesca Real-Fernandez, Feliciana Vaezi, Zahra Stella, Lorenzo Venanzi, Mariano Rovero, Paolo Papini, Anna Maria Membranes (Basel) Article 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 Glu(5) and His(9) residues on the opposite ends of the CSF114(Glc) β-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’ 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. MDPI 2015-09-30 /pmc/articles/PMC4704000/ /pubmed/26437433 http://dx.doi.org/10.3390/membranes5040576 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Becucci, Lucia Benci, Stefano Nuti, Francesca Real-Fernandez, Feliciana Vaezi, Zahra Stella, Lorenzo Venanzi, Mariano Rovero, Paolo Papini, Anna Maria Interaction Study of Phospholipid Membranes with an N-Glucosylated β-Turn Peptide Structure Detecting Autoantibodies Biomarkers of Multiple Sclerosis |
title | Interaction Study of Phospholipid Membranes with an N-Glucosylated β-Turn Peptide Structure Detecting Autoantibodies Biomarkers of Multiple Sclerosis |
title_full | Interaction Study of Phospholipid Membranes with an N-Glucosylated β-Turn Peptide Structure Detecting Autoantibodies Biomarkers of Multiple Sclerosis |
title_fullStr | Interaction Study of Phospholipid Membranes with an N-Glucosylated β-Turn Peptide Structure Detecting Autoantibodies Biomarkers of Multiple Sclerosis |
title_full_unstemmed | Interaction Study of Phospholipid Membranes with an N-Glucosylated β-Turn Peptide Structure Detecting Autoantibodies Biomarkers of Multiple Sclerosis |
title_short | Interaction Study of Phospholipid Membranes with an N-Glucosylated β-Turn Peptide Structure Detecting Autoantibodies Biomarkers of Multiple Sclerosis |
title_sort | interaction study of phospholipid membranes with an n-glucosylated β-turn peptide structure detecting autoantibodies biomarkers of multiple sclerosis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4704000/ https://www.ncbi.nlm.nih.gov/pubmed/26437433 http://dx.doi.org/10.3390/membranes5040576 |
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