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Issue 5, 2015
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Autoantigenicity of human C1q is associated with increased hydrophobicity due to conformational transitions in the globular heads

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Abstract

We analyzed the structural features of C1q that underlie its autoantigenicity by means of a model system using the amphiphilic polyzwitterion (PZ), poly(ethylene oxide-b-N,N-dimethyl(methacryloyloxyethyl) ammonium propanesulfonate) in the process of C1q immobilization. The source of anti-C1q autoantibodies was human sera from patients with Lupus Nephritis (LN). Both analyzed concentrations of PZ, 25 mM and 50 mM, were found to be applicable for inducing conformational transitions which resulted in increased recognition of C1q and the globular domain of its B polypeptide chain, designated ghB, by the LN autoantibodies. The registered conformational transitions displayed a hydrophobic enhancement of the protein microenvironment due to the presence of hydrophobic binding sites in ghB which consequently affected the autoantigenicity of the whole C1q molecule.

Graphical abstract: Autoantigenicity of human C1q is associated with increased hydrophobicity due to conformational transitions in the globular heads

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Article information


Submitted
09 Jan 2015
Accepted
17 Mar 2015
First published
18 Mar 2015

Mol. BioSyst., 2015,11, 1370-1377
Article type
Paper

Autoantigenicity of human C1q is associated with increased hydrophobicity due to conformational transitions in the globular heads

V. Stoyanova, V. Bogoeva, L. Petrova, M. Tchorbadjieva, S. Petrova, V. Georgieva, G. Georgiev, B. Deliyska, V. Vasilev and I. Tsacheva, Mol. BioSyst., 2015, 11, 1370
DOI: 10.1039/C5MB00021A

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