Experimental design of size variation in albumin nanoparticles synthesized by electron beam

Abstract

Protein-based nanoparticles have garnered significant interest for their potential in theranostic applications, including cancer treatment and nuclear medicine. Plasma proteins are particularly appealing due to their ability to bypass the rapid clearance typically associated with synthetic particles. Human serum albumin (HSA), for example, is already utilized in diagnostic procedures such as lymphoscintigraphy and sentinel lymph node detection and in cancer treatments where it delivers therapeutic agents in nanoparticulate form. Among the various techniques for synthesizing protein nanoparticles, ionizing radiation stands out for its ability to maintain good size control and preserve the protein's three-dimensional structure. Factors such as the reaction precursor, pH, protein concentration, presence of a stabilizer, and irradiation dose can all influence the size and shape of the resulting nanoparticles. This study sought to identify a correlation between the size of albumin nanoparticles and reaction parameters, including protein concentrations, the ionic content of the buffer solution, and the e-beam irradiation dose. We conducted different synthesis methods with varying BSA concentrations, using two different buffers and varying radiation doses. The resulting nanoparticles were evaluated using Dynamic Light Scattering. The size data were statistically analyzed using SAS Studio, SAS JMP, and WEKA software to identify correlations among the synthesis variables. Our observations primarily revealed that lower protein concentrations consistently resulted in smaller particles. Additionally, using Tris-HCl buffer as a medium led to a more proportional growth of particles with increases in concentration and irradiation dose. These findings suggest that Tris buffer is more suitable for BSA nanoparticle synthesis, as increased albumin concentration and radiation dose resulted in more consistent size control.