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Assembly of Nanoconjugates as New Kind Inhibitor of the Aggregation of Amyloid Peptides Associated with Alzheimer's Disease
Author(s) -
Li Chao,
Lu Jianyang,
Hu Xiaolu,
Feng Chang,
Xiang Yang,
Karamanos Yannis,
Li Genxi
Publication year - 2018
Publication title -
particle and particle systems characterization
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.877
H-Index - 56
eISSN - 1521-4117
pISSN - 0934-0866
DOI - 10.1002/ppsc.201700384
Subject(s) - aptamer , chemistry , proteolysis , protease , amyloid (mycology) , small molecule , combinatorial chemistry , peptide , protease inhibitor (pharmacology) , biochemistry , enzyme , biophysics , nanotechnology , computational biology , microbiology and biotechnology , biology , materials science , virology , inorganic chemistry , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load
The inhibition of amyloid‐β (Aβ) aggregation has been regarded as the primary therapeutic strategy for Alzheimer's diseases (AD). Currently, many kinds of amyloid inhibitors have been explored, but these inhibitors have their own drawbacks. This study proposes and demonstrates a new kind of inhibitor in this work by making use of protease endowed with high selectivity to prevent Aβ aggregation. To do this, a nanoconjugate that is composed of chymotrypsin, Aβ aptamer, and gold nanoparticle is designed and fabricated. The nanoconjugate can actively capture Aβ through interaction between the aptamer and Aβ, and destroy the target peptides through proteolysis mediated by the adjacent protease molecules. Compared with the conventional inhibitors that only passively bind with Aβ, this new kind of inhibitor may provide a novel insight to control Aβ aggregation. The multivalent binding and efficient enzymatic reaction toward Aβ may also enable a more complete clearance of Aβ, which might achieve a better treatment effect for AD in the future.