Protein nanoparticles are used to carry and deliver drugs to disease tissues. They constitute an alternative to classical protein–ligand complexes and Emodin is a novel drug that displays interesting anticancer activities. We have characterized an albumin (BSA) nanoparticle obtained by gamma irradiation and studied the influence of Emodin- nanoparticle–BSA interactions over the protein bioconjugate Emodin–BSA, related to the protein structure by TEM, light scattering, and pH influence by UV-Vis, FTIR and steady-state fluorescence. Besides, its impact on in vivo toxicity, covering morphology, cardiotoxicity, DL50 and compartmental studies on zebrafish model was studied.
The drug was found to induce structural changes on the protein nanoparticle. In particular, secondary structure diminishes, and complexes formed in the presence of nanoparticles are more stable than those formed by the protein itself (Emodin-BSA bioconjugates) in water solution. Also, the amount of drug molecules interacting with the protein is higher when the nanoparticle is present.
The most significant changes of biotoxicity were observed when zebrafish larvae were treated with free Emodin, and no significant changes were observed when larvae were treated with the complex. Biotoxicity is discussed in depth analyzing actual controversies on nanoparticles toxicity under present regulatory dispositions.
The results presented here will help to further understand the nanoparticles–protein–drug interactions and the role that Emodin-BSA nanoparticles may play in biomedical and pharmacological applications.
Acknowledgements:UNQ, MINCyT, CONICET, FAN