Nanoparticles interacting with a protein strand, showing influence of electric charges.

Nanoparticle Breakthrough: Can Charged Surfaces Stop Protein Fibrillation?

Beau Callahan in Science & Nature November 2025 • 5 min read.

"New research explores how engineered nanoparticles with varying electric charges can influence the behavior of albumin protein, potentially opening doors for novel biomedical applications."

Nanoparticles are revolutionizing numerous fields, from medicine to materials science. Their incredibly small size allows them to interact with biological systems at a molecular level, offering unprecedented opportunities for targeted drug delivery, advanced diagnostics, and innovative therapies. However, understanding how these tiny particles interact with the complex biological environment is crucial for ensuring their safe and effective use.

A key area of interest is the interaction between nanoparticles and proteins, the workhorses of our cells. Proteins perform a vast array of functions, and their behavior can be influenced by their surrounding environment. When proteins misfold and aggregate, a process known as fibrillation, it can lead to various diseases, including neurodegenerative disorders. Therefore, researchers are exploring whether nanoparticles can be engineered to prevent or even reverse protein fibrillation.

Recent research has focused on using superparamagnetic iron oxide nanoparticles (SPIONs) as a tool to manipulate protein behavior. By coating these nanoparticles with different electric charges, scientists can control how they interact with proteins like albumin, a major protein found in blood. A new study investigates how these charged nanoparticles affect the fibrillation of albumin, potentially providing insights into new therapeutic strategies.

Charged Nanoparticles: A Novel Approach to Controlling Protein Behavior

Nanoparticles interacting with a protein strand, showing influence of electric charges.

The study, conducted by researchers at the National Institute of Genetic Engineering and Biotechnology in Iran, explores the impact of surface charge on SPIONs and their interaction with albumin protein. The researchers synthesized SPIONs and coated them with varying electric charges using different concentrations of glycine during the synthesis process. This allowed them to create nanoparticles with distinct surface properties, enabling them to investigate how these differences affected albumin fibrillation.

The researchers used a reverse co-precipitation method to synthesize the SPIONs. This method involves carefully mixing iron salts in an alkaline solution under controlled conditions to form nanoparticles. The size and chemical properties of the nanoparticles were then characterized using transmission electron microscopy (TEM), vibrating sample magnetometry (VSM), and X-ray diffraction (XRD).

Transmission Electron Microscopy (TEM): This technique provided high-resolution images of the nanoparticles, allowing the researchers to determine their size and shape.
Vibrating Sample Magnetometry (VSM): VSM was used to measure the magnetic properties of the nanoparticles, confirming their superparamagnetic nature.
X-Ray Diffraction (XRD): XRD analysis revealed the crystalline structure of the nanoparticles, confirming the presence of iron oxide crystals.

To investigate the impact of the charged nanoparticles on albumin fibrillation, the researchers incubated the protein with different types of SPIONs and then subjected the mixture to heat. The extent of fibrillation was then measured using a thioflavin T (THT) assay, a common method for detecting amyloid fibrils. The study found that nanoparticles with different surface charges had varying effects on albumin fibrillation. This suggests that controlling the surface charge of nanoparticles could be a viable strategy for modulating protein behavior.

Future Directions: Engineering Nanoparticles for Therapeutic Applications

This research provides valuable insights into the complex interactions between nanoparticles and proteins, highlighting the importance of surface charge in modulating protein behavior. By carefully engineering the surface properties of nanoparticles, it may be possible to develop targeted therapies for diseases associated with protein misfolding and aggregation.

Further studies are needed to fully elucidate the mechanisms by which charged nanoparticles influence protein fibrillation. Future research could also explore the use of different types of nanoparticles and surface modifications to optimize their therapeutic potential. Understanding the long-term effects of nanoparticle exposure on biological systems is also crucial for ensuring their safe and effective use.

Ultimately, the ability to control protein behavior with nanoparticles holds great promise for treating a wide range of diseases, from neurodegenerative disorders to cancer. This research represents an important step towards realizing that potential.

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This article is based on research published under:

DOI-LINK: 10.1016/j.dib.2018.10.170, Alternate LINK

Title: Dataset On The Relation Of Synthetic Super Para Magnetic Nanoparticles Coated With Various Electric Charges And Fibrillation Of Albumin Protein

Subject: Multidisciplinary

Journal: Data in Brief

Publisher: Elsevier BV

Authors: Negin Javdani, Sayyed Shahryar Rahpeyma, Younes Ghasemi, Jamshid Raheb

Published: 2018-12-01

Everything You Need To Know

What are nanoparticles and why are they being studied in this context?

Engineered nanoparticles, particularly superparamagnetic iron oxide nanoparticles (SPIONs), are being used to study and potentially control protein behavior. These nanoparticles, due to their incredibly small size, can interact with biological systems at a molecular level. By modifying the surface charge of these SPIONs, scientists are investigating how they interact with proteins like albumin, which is a major protein found in blood. The goal is to understand and manipulate protein fibrillation, which is the misfolding and aggregation of proteins, leading to various diseases.

What is protein fibrillation and why is it relevant to this research?

Protein fibrillation is a process where proteins misfold and aggregate, potentially leading to various diseases, including neurodegenerative disorders. The study focuses on the interaction between synthetic nanoparticles and albumin protein. By understanding and controlling protein fibrillation, researchers aim to develop new therapeutic strategies for diseases associated with protein misfolding and aggregation.

Why is the surface charge of nanoparticles significant in this study?

The surface charge of superparamagnetic iron oxide nanoparticles (SPIONs) is important because it influences how these nanoparticles interact with proteins like albumin. Researchers can control the surface charge of SPIONs by coating them with different electric charges during the synthesis process. This allows them to investigate how these distinct surface properties affect albumin fibrillation, potentially providing insights into new therapeutic strategies for diseases associated with protein misfolding.

What methods did the researchers use to analyze the nanoparticles?

The researchers used several techniques to characterize the superparamagnetic iron oxide nanoparticles (SPIONs). Transmission Electron Microscopy (TEM) provided high-resolution images to determine their size and shape. Vibrating Sample Magnetometry (VSM) was used to measure their magnetic properties, confirming their superparamagnetic nature. X-Ray Diffraction (XRD) analysis revealed the crystalline structure, confirming the presence of iron oxide crystals.

What are the potential future implications of this research?

The research has implications for developing targeted therapies for diseases associated with protein misfolding and aggregation. By controlling the surface charge of nanoparticles, scientists may be able to prevent or even reverse protein fibrillation. This could lead to new treatments for conditions like neurodegenerative disorders. Future research could focus on engineering nanoparticles for therapeutic applications, using the insights gained from studying the interaction between nanoparticles and albumin protein.