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Journal Article

Randomization of amyloid-β-peptide(1-42) conformation by sulfonated and sulfated nanoparticles reduces aggregation and cytotoxicity

MPS-Authors
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Saraiva,  A. M.
Grenzflächen, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Tauer,  K.
Klaus Tauer, Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Möhwald,  H.
Helmuth Möhwald, Grenzflächen, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Brezesinski,  G.
Gerald Brezesinski, Grenzflächen, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

Saraiva, A. M., Cardoso, I., Saraiva, M. J., Tauer, K., Pereira, M. C., Coelho, M. A. N., et al. (2010). Randomization of amyloid-β-peptide(1-42) conformation by sulfonated and sulfated nanoparticles reduces aggregation and cytotoxicity. Macromolecular Bioscience, 10(10), 1152-1163. doi:10.1002/mabi.200900448.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-4A78-B
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