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Conformational structure of the MOG‐derived peptide 101–108 in solution
Author(s) -
Guardiani Carlo,
Marsili Simone,
Marchetti Stefania,
Gambi Cecilia,
Procacci Piero,
Livi Roberto
Publication year - 2011
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21510
Subject(s) - myelin oligodendrocyte glycoprotein , chemistry , peptide , circular dichroism , autoantibody , antibody , decoy , multiple sclerosis , crystallography , biochemistry , immunology , experimental autoimmune encephalomyelitis , receptor , biology
One of the most important targets in the autoimmune attack in experimental autoimmune encephalomyielitis is the myelin oligodendrocyte glycoprotein (MOG). The complex with demyelinating 8‐18C5 antibody was recently resolved by X‐ray crystallography, showing a remarkable adhesion of the 101–108 MOG subsequence to the heavy chain of the autoantibody. In this study, we have determined, using replica exchange molecular dynamics methods, the structure of the MOG‐derived peptide 101–108 in solution at ambient conditions. According to the simulation, the peptide exhibits, with significant probability, a distorted β‐turn structure highly similar to that of the corresponding subsequence in the crystal in complex with 8‐18C5 antibody. Such results are found to be fully consistent with circular dichroism spectra of the peptide in solution, suggesting the use of the MOG‐derived 101–108 peptide as a potential lead compound for designing decoy targets for the autoimmune attack in multiple sclerosis. © 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 96: 245–251, 2011.