Characterization of a Protein Nanoparticle, Bsanano and its Interaction With-Emodin

MACARENA SIRI; A. LIS FEMIA; MARIA JULIETA FERNANDEZ RUOCCO; NADIA S. CHIARAMONI; GONZALO CASAJUS; MARIANO GRASSELLI; SILVIA DEL V. ALONSO

Philapelphia

Congreso; 57th Annual Meeting Biophysical Society; 2013

BSA nanoparticles (BSAn) and Emodin, as BSAn:Emodín bioconjugate characteristics and binding activity was examined by spectroscopy and release kinetics assays. BSAn:Emodin was characterized by column chromatography, light scattering, UV-Vis, FTIR, and electron microscopy (TEM). Interaction between BSAn and emodin was analysed by docking-release technology.BSAn and Emodin binding characteristics were determined by different biophysical methods. Binding release is slower and longer controlled release than molecular BSA:Emodin complex. FTIR measurements indicate an increase in the α-helical content of the protein and a change in the environment of the tryptophan residues which are located inward, buried in the hydrophobic interior of the biomolecule. This variation on the secondary structure could have further influence in the binding of the drug to form transport and regulatory complexes. Our findings point out that BSAn has more potency than BSA agent in delivering anticancer drug Emodin.We also studied the effect of the BSAn bound to the anitumoral drug Emodin, on the activity of zebrafish larvae. Emodin presents great toxicity. Almost no effect was observed in larvae treated with the complex BSAn:Emodin. These were also compared to larvae exposed to BSA and BSA:Emodin. The BSA showed a great hyperactivity on the larvae, whereas the complex, seemed to cause a toxic effect similar to the one caused by the drug alone.