NRF(National Research Foundation of Korea)

Achievements
Latest News Releases
Decoding the Roles of Amyloid-β (1-42)’s Key Oligomerization Domains toward Designing Epitope-Specific Aggregation Inhibitors
Writer 고홍숙
Date 2023-07-21 13:10:34.0
Hit 222

The accumulation of amyloid-β (Aβ) and the microtubule-associated protein tau are the pathological hallmarks of Alzheimer's disease (AD). The formation of senile plaques in the brains of AD patients is a result of fibrillar amyloid aggregation of Aβ. Researchers at Korea University and Pusan National University rationally designed candidate drugs using a machine learning algorithm that predicts the binding sites of designed peptides against prefibrillary Aβ. Furthermore, the researchers report the key oligomerization domains of Aβ. The study appears in JACS Au in March.

   

The researchers confirmed the suppressive effects of the inhibitor candidates on amyloid aggregate formation and Aβ-dependent cytotoxicity in vitro and investigated the interference of inhibitor candidates in early-stage aggregation using an interdisciplinary biophysical approach.

   

Prof. Kim said that “Our findings that posit the roles of each hydrophobic domain during the Aβ oligomerization can be applied to the development of novel therapeutic agents for AD.”



“Decoding the Roles of Amyloid-β (1-42)‘s Key Oligomerization Domains toward Designing Epitope-Specific Aggregation Inhibitors” by Hugh I. Kim (published by American Chemical Society) is licensed under CC BY 4.0



[Reference] Im D. et al., Decoding the Roles of Amyloid-β (1-42)’s Key Oligomerization Domains toward Designing Epitope-Specific Aggregation Inhibitors, JACS Au, https://doi.org/10.1021/jacsau.2c00668

[Main Author] Dongjoon Im(Korea University), Hugh I. Kim(Korea University), Jeong-Mo Choi (Pusan National University)

* Contact : Professor Hugh I. Kim (hughkim@korea.ac.kr), Professor Jeong-Mo Choi (jeongmochoi@pusan.ac.kr)