This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Alzheimer's disease is a neurodegenerative brain disorder characterized by progressive memory loss and a decline in other mental functions. Past studies have consistently linked this disorder to the accumulation of the protein amyloid-β (Aβ) between brain cells, ultimately resulting in the formation of so-called amyloid plaques.
Amyloid plaques can disrupt communication between cells, cause inflammation and damage crucial connections in the brain, eventually prompting the death of neurons and the symptoms associated with Alzheimer's disease. Once they have formed, these protein clumps are very difficult to remove using conventional therapeutic and surgical strategies. Researchers at Nankai University and Hebei University of Technology nanoengineered a new material that could help dismantle amyloid plaques in the brain.
This material, presented in a paper published in Nature Nanotechnology, combines the naturally occurring protein ferritin with tiny clusters of gold (Au) atoms. "The idea for this work originated from an unexpected observation during our research," Xinglu Huang, senior author of the paper, told Tech Xplore. "We found that ferritin nanocage-Au hybrid nanomaterials were able to disrupt preformed Aβ aggregates.
This finding intrigued us because several inorganic nanomaterials had previously been reported to interfere with Aβ aggregation. However, through an extensive review of the literature, we realized that these materials most likely act through nonspecific interactions with protein aggregates." After reviewing earlier studies, the researchers set out to nanoengineer and evaluate a new material combining ferritin and Au nanocages. While they had already gathered some insight hinting at the potential of this material for disassembling amyloid plaques, the molecular mechanisms through which it acted on the protein clumps remained poorly understood.
"In addition, these materials' limited biocompatibility and translational potential have so far made in vivo applications challenging," explained Huang. "Building on these observations, we tried to engineer a bioactive nanostructure that specifically recognizes Aβ aggregates and actively remodels them through a well-defined molecular mechanism. Inspired by the precise molecular recognition capabilities of biological systems, we selected ferritin nanocages as a biocompatible and programmable protein scaffold and computationally engineered them with Aβ-targeting modules to create a bioactive nanostructure capable of selectively engaging Aβ aggregates." Unlike conventional inorganic nanomaterials, the material introduced by Huang and his colleagues was designed to recognize specific molecules and enter living organisms without disrupting vital physiological processes.
The team's initial priority was to ensure that their nanomaterial could reliably recognize and target Aβ aggregates instead of interacting with other proteins and healthy cells. "We genetically engineered a human ferritin nanocage by displaying computationally optimized Aβ-recognition peptides on its surface, thereby endowing the nanostructure with the ability to selectively target Aβ aggregates," said Huang. "The ferritin scaffold not only provides excellent biocompatibility but also serves as a programmable platform for precisely organizing the targeting ligands and gold nanostructures." Discover the latest in science, tech, and space with over 100,000 subscribers who rely on Phys.org for daily insights. d research that matter—daily or weekly.
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