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Zinc binding agonist effect on the recognition of the β-amyloid (4–10) epitope by anti-β-amyloid antibodies

Zinc binding agonist effect on the recognition of the β-amyloid (4–10) epitope by anti-β-amyloid antibodies

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ZIRAH, Séverine, Raluca STEFANESCU, Marilena MANEA, Xiaodan TIAN, Roxana CECAL, Sergey A. KOZIN, Pascale DEBEY, Sylvie REBUFFAT, Michael PRZYBYLSKI, 2004. Zinc binding agonist effect on the recognition of the β-amyloid (4–10) epitope by anti-β-amyloid antibodies. In: Biochemical and Biophysical Research Communications. 321(2), pp. 324-328. ISSN 0006-291X

@article{Zirah2004-08-20bindi-17609, title={Zinc binding agonist effect on the recognition of the β-amyloid (4–10) epitope by anti-β-amyloid antibodies}, year={2004}, doi={10.1016/j.bbrc.2004.06.150}, number={2}, volume={321}, issn={0006-291X}, journal={Biochemical and Biophysical Research Communications}, pages={324--328}, author={Zirah, Séverine and Stefanescu, Raluca and Manea, Marilena and Tian, Xiaodan and Cecal, Roxana and Kozin, Sergey A. and Debey, Pascale and Rebuffat, Sylvie and Przybylski, Michael} }

Stefanescu, Raluca Cecal, Roxana Publ. in: Biochemical and biophysical research communications ; 321 (2004), 2. - S. 324-328 Debey, Pascale Kozin, Sergey A. Stefanescu, Raluca Manea, Marilena Amyloid plaques associated to Alzheimer’s disease present a high content of zinc ions. We previously showed that the N-terminal region of the amyloid peptide Aβ constitutes an autonomous zinc-binding domain. This region encompasses the previously identified epitope Aβ(4–10) targeted by antibodies capable to reduce amyloid deposition, but the influence of Aβ/Zn binding on the epitope recognition remains unknown. We demonstrate here the effect of Zn<sup>2+</sup> ions on the recognition of peptides sharing the sequence of the Aβ N-terminal domain, by two monoclonal antibodies recognizing the β-amyloid(4–10) epitope. The presence of Zn<sup>2+</sup>, but not of other cations, increased the recognition of the (1–16) peptide, while it was without effect on the recognition of the (1–10) peptide. These findings show a zinc-induced conformational change of the (1–16)-N-terminal region of Aβ, which results in a better accessibility of the Aβ(4–10) epitope to the anti-Aβ antibodies, and suggest a role of zinc in epitope-based vaccination approaches. Kozin, Sergey A. 2012-02-01T09:04:39Z Przybylski, Michael 2004-08-20 Cecal, Roxana Przybylski, Michael Zinc binding agonist effect on the recognition of the β-amyloid (4–10) epitope by anti-β-amyloid antibodies 2012-02-01T09:04:39Z eng Tian, Xiaodan Rebuffat, Sylvie Zirah, Séverine Debey, Pascale Tian, Xiaodan Manea, Marilena Zirah, Séverine deposit-license Rebuffat, Sylvie

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