The World Health Organization estimates that 50 million people worldwide battle neurodegenerative disorders — and that number should increase as our population ages. 

At Missouri State University, Dr. Tuhina Banerjee’s research offers promising insight on potentially revolutionizing treatment approaches for these conditions. 

Banerjee is an assistant professor of chemistry and biochemistry. Soon after joining the university in 2021, she began her research on insulin with a team of students. 

Banerjee’s research, “Mechanistic Insights Behind the Self-Assembly of Human Insulin under the Influence of Surface-Engineered Gold Nanoparticles” was recently published in ACS Chemical Neuroscience. Graduate students Zachary Flint, Haylee Grannemann, Kristos Baffour and Neelima Koti played a pivotal role in driving the success of this innovative research project.

“Without their hard work, this publication would not have been possible,” Banerjee said. 

About ACS Chemical Neuroscience 

ACS Chemical Neuroscience is a monthly peer-reviewed scientific journal published by the American Chemical Society (ACS). It focuses on research at the interface of chemistry and neuroscience, covering a broad range of topics related to the molecular mechanisms of neurological disorders.  

The journal publishes original research articles, reviews and editorials in these areas. It provides a platform for scientists to share their findings and contribute to advancements in the field of chemical neuroscience. 

“As a researcher, I’ve always wanted to venture into protein misfolding diseases associated with neurodegenerative diseases,” Banerjee said. “Due to MSU’s support in my research and other facilities, my lab was successful in this effort.”  

More about the research 

The focus of Banerjee’s research is on understanding the aggregation dynamics of proteins associated with neurodegenerative diseases, such as Parkinson’s and Alzheimer’s. 

Specifically, her team is examining the self-assembly of human insulin under the influence of surface-engineered gold nanoparticles. 

They chose insulin as a model protein for their research due to its structural similarities to proteins implicated in neurodegenerative diseases, such as alpha-synuclein and amyloid beta. 

The study found that modifying gold nanoparticles with hierarchical polyethylene glycol (PEG) structures influences how insulin proteins clump together into amyloid fibrils. Larger PEG molecules on the nanoparticles enhanced the formation of these fibrils, which are associated with diseases like Alzheimer’s.

This fibril formation also reduced the toxicity of insulin clumps. The research suggests that tailoring nanoparticle surfaces could offer new ways to treat diseases involving amyloid proteins. 

Banerjee and her team plan to continue their research with the goal of explaining the molecular mechanisms underlying protein aggregation and exploring novel therapeutic interventions.  

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