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Updated: Dec 23, 2025

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
Disassembling and degradation of amyloid protein aggregates based on gold nanoparticle-modified g-C3N4
Jie Wang1, Yonghai Feng1, Xiaohua Tian1
1Institute for Advanced Materials, School of Material Science and Engineering, Jiangsu University, Zhenjiang 212013, China.
Abstract:
Amyloid protein misfolds, abnormally aggregates and accumulates into amyloid deposits which endanger tissue functions and are closely related to the pathogenesis of many diseases including Type 2 Diabetes Mellitus (T2DM). There are on-going efforts to find new methods or effective reagents to disassemble and eliminate the existing amyloid aggregates. Herein, we showed that a gold nanoparticle-modified quasi-2D nanomaterial, Au/g-C3N4, could efficiently degrade preformed amyloid aggregates. Furthermore, the scavenger experiment revealed this photodegradation effect was depended on the induced oxygen radicals, particularly hydroxyl radical. The new finding in this work could demonstrate that a gold nanoparticle-modified quasi-2D nanomaterial would have potential applications in the strategy design of the treatment of amyloid related diseases in future.

