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Inside Cover: Surface‐Modified Protein Microspheres Capture Amyloid‐β and Inhibit its Aggregation and Toxicity (Chem. Eur. J. 40/2011)
Author(s) -
Richman Michal,
Wilk Sarah,
Skirtenko Natalia,
Perelman Alex,
Rahimipour Shai
Publication year - 2011
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201190196
Subject(s) - chemistry , microsphere , toxicity , peptide , selectivity , amyloid β , amyloid (mycology) , protein aggregation , biophysics , surface protein , amyloid fibril , biochemistry , disease , chemical engineering , biology , medicine , organic chemistry , virology , engineering , inorganic chemistry , catalysis
Accumulation and aggregation of amyloid‐β (Aβ) in the brain is the primary pathogenic event in Alzheimer's disease (AD). Thus reducing the level of Aβ in the brain is considered to be a promising strategy for AD therapy. In their Full Paper on page 11171 ff. , S. Rahimipour et al. describe sonochemically prepared protein microspheres, the surfaces of which are modified with an Aβ recognition peptide. The microspheres can bind with high affinity and selectivity to Aβ, sequester it from the medium, inhibit its aggregation, and directly reduce its toxicity toward neuron‐like cells.