Correlation between assembly structure of a gamma irradiated albumin nanoparticle and its function as a drug delivery system

Abstract

The present study correlates the structure of an albumin nanoparticle with its function as a drug delivery system. The albumin nanoparticle was created by a clean and size-controlled desolvation method in combination with gamma irradiation as a cross-linker. It is composed of 3950 albumin molecules with a molecular weight of 5.78E + 02 MDa and the binding between the albumin molecules creates new hydrophobic pockets. Our hypothesis was that the very assembly structure of the nanoparticle played a key role in making it a suitable drug delivery system. In order to study how the assembly of the nanoparticle enhanced its function as such, we used a hydrophobic drug, Emodin. The high affinity of the nanoparticle for the drug was studied with spectroscopy. We found that the nanoparticle's many hydrophobic pockets improved the encapsulation efficiency of the system. In cell toxicity and haemolysis experiments, the nanoparticle's toxicity levels were low. These results suggest that the nanoparticle has great potential as a drug delivery system.