In my comprehensive study on the electrokinetic properties of bovine serum albumin (BSA) in potassium chloride solutions, I focused on the intricate effects of high salt concentrations and pH levels, aiming to deepen the understanding of protein behavior in aqueous environments, with a particular emphasis on zeta potential, which is vital in the realms of nanoparticle-medication interactions, protein adsorption, and stability in various environments.

Key Aspects of My Study:
    1. Electrode Material Selection: One of my significant findings was the impact of electrode material on the quality of electrophoretic light scattering (ELS) measurements. I discovered that using platinized platinum electrodes, as opposed to palladium or platinum, is crucial to avoid interference from electrochemical phenomena at the electrode-liquid interface. This choice of material is essential for obtaining accurate and reliable results.
    2. Electrophoretic Mobility and Protein Charge: In my research, I meticulously quantified the protonic charge per protein molecule through potentiometric acid titration and correlated these findings with electrophoretic mobility measurements. This approach provided a clearer understanding of protein behavior under various pH levels, revealing important insights into protein charge dynamics.
  1. Importance of Electrokinetic Models: I found that selecting appropriate electrokinetic models for accurate prediction of electrophoretic mobilities is especially critical in high salt conditions. In such environments, protein behavior becomes more complex, making it crucial for accurately determining zeta potential, a key parameter in understanding nanoparticle and protein interactions.
  2. Protein Behavior in Aqueous Solutions: My study showed that BSA behaves as a permeable polyelectrolyte in potassium chloride solutions. This behavior is influenced by protonation, chloride counterion binding, and the inherent permeability of the protein molecules, leading to intricate interactions and charge dynamics.
  3. Interactions in High Ionic Strength Environments: I delved into how proteins interact in high ionic strength solutions, affected by variables like pH and electrolyte concentration. These interactions play a crucial role in determining the net charge and mobility of the protein molecules.
  4. Nanomedicine Applications: The detailed analysis of protein behavior in different ionic strengths and pH levels has substantial implications for nanomedicine. Understanding the protein corona formation and adsorption at interfaces is vital for developing effective nanoparticle-based drugs and therapies.
  5. Recommendations for ELS Analysis: My study advocates for careful consideration of experimental conditions, such as electrode material and model selection, for accurate ELS analysis of proteins. This is crucial for reliable characterization of their electrokinetic properties in varied environments.

In conclusion, my research provides essential insights into protein behavior in “high salt” conditions and underlines the significance of methodological choices in electrophoretic mobility measurements. This work is a valuable contribution to the fields of protein chemistry, colloidal science, and particularly nanomedicine, where understanding protein interactions at the nanoscale is critical.

Miller, J. F. Determination of Protein Charge in Aqueous Solution Using Electrophoretic Light Scattering: A Critical Investigation of the Theoretical Fundamentals and Experimental Methodologies. Langmuir 2020, 36 (29), 8641–8654.


You should see the original PDF in a viewer below but on Microsoft Edge you may see a Microsoft Defender SmartScreen warning. This is a false positive that has been reported to Microsoft. Please use the link above to access the PDF.

Leave a Reply

Your email address will not be published. Required fields are marked *

This site uses Akismet to reduce spam. Learn how your comment data is processed.