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Cover Picture: Controlling Amyloid‐β Peptide(1–42) Oligomerization and Toxicity by Fluorinated Nanoparticles (ChemBioChem 13/2010)
Author(s) -
Saraiva Ana M.,
Cardoso Isabel,
Pereira M. Carmo,
Coelho Manuel A. N.,
Saraiva Maria João,
Möhwald Helmuth,
Brezesinski Gerald
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201090061
Subject(s) - chemistry , amyloid fibril , peptide , biophysics , intermolecular force , nanoparticle , amyloid (mycology) , fibril , beta sheet , combinatorial chemistry , hydrophobic effect , amyloid disease , nanotechnology , amyloid β , biochemistry , organic chemistry , molecule , materials science , biology , disease , medicine , inorganic chemistry , pathology
The cover picture shows that dynamic fluorinated nanoparticles (NPs) induce α‐helix‐rich structures in Alzheimer's disease Aβ peptides and prevent aggregation, whereas their hydrogenated analogues are less efficient, leading to β‐sheet formation and fibrillation. Moreover, fluorinated NPs exert antioligomeric and antiapoptotic effects, thereby increasing the viability of human neuroblastoma cells treated with Aβ oligomeric species. The hydrogenated NPs, however, have the opposite effect, inducing the formation β‐sheet‐enriched structures that are more prone to aggregate and more cytotoxic. The proper balance between hydrophilic moieties that allow solubility and hydrophobic chains to exploit the intermolecular interactions of Aβ assembly seems to be an essential feature of effective NPs. The results presented could contribute to the development of new approaches for the study of protein‐misfolding diseases and therapy. For more information, see the paper by A. N. Saraiva, G. Brezesinski et al. on p. 1905 ff.