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- W1976598442 abstract "Alzheimer's disease (AD) is the most common form of dementia and currently affects 5.4 million Americans. A number of anti-Aβ (beta amyloid) therapeutic agents have been developed for AD, but so far all of them failed in clinic. Here we used peptoid chemistry to develop ligands selective for Aβ42. Peptoids are N-substituted glycine oligomers, a class of peptidomimics. We synthesized an on-bead peptoid library consisting of 38,416 unique peptoids. The generated peptoid library was screened and arrays of Aβ42-selective peptoid ligands were identified. One of those peptoid ligands, IAM1 (inhibitor of amyloid), and the dimeric form (IAM1)2 were synthesized and evaluated in a variety of biochemical assays. We discovered that IAM1 selectively binds to Aβ42, while the dimeric derivative (IAM1)2 has a higher affinity for Aβ42. Furthermore, we demonstrated that IAM1 and (IAM1)2 were able to inhibit the aggregation of Aβ42 in a concentration-dependent manner, and that (IAM1)2 protected primary hippocampal neurons from the Aβ-induced toxicity in vitro. These results suggest that IAM1 and (IAM1)2 are specific Aβ42 ligands with antiaggregation and neuroprotective properties. IAM1, (IAM1)2, and their derivatives hold promise as Aβ42 detection agents and as lead compounds for the development of AD therapeutic agents." @default.
- W1976598442 created "2016-06-24" @default.
- W1976598442 creator A5003791840 @default.
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- W1976598442 date "2013-03-07" @default.
- W1976598442 modified "2023-10-16" @default.
- W1976598442 title "Aβ42-Binding Peptoids as Amyloid Aggregation Inhibitors and Detection Ligands" @default.
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- W1976598442 doi "https://doi.org/10.1021/cn400011f" @default.
- W1976598442 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3689191" @default.
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