University of Oulu

Tuusa, J., Raasakka, A., Ruskamo, S. et al. Myelin-derived and putative molecular mimic peptides share structural properties in aqueous and membrane-like environments. Mult Scler Demyelinating Disord 2, 4 (2017).

Myelin-derived and putative molecular mimic peptides share structural properties in aqueous and membrane-like environments

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Author: Tuusa, Jussi1; Raasakka, Arne1,2; Ruskamo, Salla1;
Organizations: 1Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Oulu, Finland
2Department of Biomedicine, University of Bergen, Bergen, Norway
Format: article
Version: published version
Access: open
Online Access: PDF Full Text (PDF, 3.2 MB)
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Language: English
Published: Springer Nature, 2017
Publish Date: 2021-03-24


Background: Despite intense research, the causes of various neurological diseases remain enigmatic to date. A role for viral or bacterial infection and associated molecular mimicry has frequently been suggested in the etiology of neurological diseases, including demyelinating autoimmune disorders, such as multiple sclerosis. Pathogen mimics of myelin-derived autoimmune peptides have been described in the literature and shown to induce myelin autoimmune responses in animal models.

Methods: We carried out a structural study on myelin-derived peptides, and mimics thereof from various pathogens, in aqueous and membrane-like environments, using conventional and synchrotron radiation circular dichroism spectroscopy. A total of 13 peptides from the literature were studied, and 290 circular dichroism spectra were analysed. In addition, peptide structure predictions and vesicle aggregation assays were performed.

Results: The results indicate a high level of similarity in the biophysical and folding properties of the peptides from either myelin proteins or proteins from pathogenic viruses or bacteria; essentially all of the studied peptides folded in the presence of lipid vesicles or under other membrane-mimicking conditions, which is a sign of membrane interaction. Many of the peptides presented remarkable similarities in their conformation in different environments.

Conclusions: As most of the studied epitope segments in myelin proteins are associated with membrane-binding sites, our results support a view of molecular mimicry, involving lipid membrane interaction propensity and similar conformational properties, possibly playing a role in demyelinating disease. The results suggest mechanisms related to protein amphiphilicity and order-disorder transitions in the recognition of peptide epitopes in autoimmune demyelination.

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Series: Multiple sclerosis and demyelinating disorders
ISSN: 2056-6115
ISSN-E: 2056-6115
ISSN-L: 2056-6115
Volume: 2
Article number: 4
DOI: 10.1186/s40893-017-0021-7
Type of Publication: A1 Journal article – refereed
Field of Science: 1182 Biochemistry, cell and molecular biology
3112 Neurosciences
3111 Biomedicine
Funding: This study has been supported by the Emil Aaltonen Foundation (Finland), the Sigrid Jusélius Foundation (Finland), the Academy of Finland, and the Research Council of Norway (SYNKNØYT program). The funders had no role in the design of the study, the collection, analysis, and interpretation of data, or in writing the manuscript.
Copyright information: © The Author(s). 2017. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (, which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( applies to the data made available in this article, unless otherwise stated.