Randomization of Amyloid-β-Peptide(1-42) Conformation by Sulfonated and 
Sulfated Nanoparticles Reduces Aggregation and Cytotoxicity

Saraiva, A. M.; Cardoso, I.; Saraiva, M. J.; Tauer, K.; Pereira, M. C.; Coelho, M. A. N.; Möhwald, H.; Brezesinski, G.

doi:10.1002/mabi.200900448

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Randomization of Amyloid-β-Peptide(1-42) Conformation by Sulfonated and Sulfated Nanoparticles Reduces Aggregation and Cytotoxicity

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

/persons/resource/persons121928

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

/persons/resource/persons121654

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

/persons/resource/persons121172

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

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Saraiva, A. M., Cardoso, I., Saraiva, M. J., Tauer, K., Pereira, M. C., Coelho, M. A. N., Möhwald, H., & Brezesinski, G. (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.

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

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