Structural studies with the uveopathogenic peptide M derived from retinal S-antigen

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DOIResolve DOI: http://doi.org/10.1021/bi00464a006
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TypeArticle
Journal titleBiochemistry
ISSN0006-2960
1520-4995
Volume29
Issue12
Pages29252930
AbstractThe 18-residue fragment of bovine S-antigen, corresponding to amino acid positions 303-320, is highly immunogenic and is known to induce experimental autoimmune uveitis. The solution conformation of this immunogenic peptide, known as peptide M, was studied by Fourier-transform infrared spectroscopy and by circular dichroism. In the pH range between approximately 4 and 9.5, peptide M has a strong tendency to form macromolecular assemblies in which it adopts an intermolecular β-sheet structure. The intermolecular β-sheets are stabilized by ionic interactions ("salt bridges") between the carboxylate groups and basic residues of the neighboring peptide molecules. These interactions can be disrupted by neutralization of either acidic (pH range below 4) or basic residues (pH range above 9.5) or by elevated hydrostatic pressure. The secondary structure of the peptide under conditions favoring the monomeric state appears to be a mixture of unordered structure and β-sheets. The present data are consistent with a recently proposed model [Sette, A., Buns, S., Colon, S., Smith, J. A., Miles, C., & Grey, H. M. (1987) Nature 328, 395-399], which assumes that certain immunogenic peptides adopt an extended β-type conformation in which they are "sandwiched" between the major histocompatibility complex and the T-cell receptor.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
NRC number30574
NPARC number23001510
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Record identifier3cd983dc-af63-4a2f-a0ee-2eeaa01fabd7
Record created2017-02-20
Record modified2017-02-20
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