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Inside Cover: Inhibition of Amyloid Peptide Fibrillation by Inorganic Nanoparticles: Functional Similarities with Proteins (Angew. Chem. Int. Ed. 22/2011)
Author(s) -
Yoo Seong Il,
Yang Ming,
Brender Jeffrey R.,
Subramanian Vivekanandan,
Sun Kai,
Joo Nam Eok,
Jeong SooHwan,
Ramamoorthy Ayyalusamy,
Kotov Nicholas A.
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201102689
Subject(s) - peptide , amyloid (mycology) , fibrillation , chemistry , alzheimer's disease , amyloid fibril , biochemistry , biophysics , pharmacology , disease , medicine , amyloid β , biology , atrial fibrillation , inorganic chemistry
Amyloid peptide fibrillation causes many neurodegenerative disorders including Alzheimers disease. Some drugs can inhibit this process by binding to peptides in a 1:1 ratio. In their Communication on page 5110 ff., N. A. Kotov et al. describe the inhibition efficacy of nanoparticles (NPs), which bind to peptide oligomers. The mechanism of NP inhibition is similar to that of proteins responsible for preventing amyloid fibrillation in the human body.