Characterization of a nanoparticle protein bioconjugate: BSAnano-Emodin drug delivery system

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

Buzios

Congreso; II Latin American Federation of Biophysical Societies (LaFeBS) Congress/ XXXVII Brazilian Biophysical Society Congress; 2012

Cell suspension and invasion is a crucial step in the metastatic cascade of cancer cells, and interruption of this step is considered to be a logical strategy for prevention and treatment of tumor metastasis. Emodin is the major active component of the rhizome of Rheum palmatum L., with known anticancer activities. Herein the effects of a plant anthraquinone, emodín bound to a BSA nanoparticle formed by γ-irradiated BSA molecules was obtained in order to produce a new possible antimetastasic drug.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 technologyBSAn and Emodin binding characteristics were determined by different biophysical methods. Binding release is slower and longer controlled release than molecular BSA:Emodin complex. Being the BSA:Emodin release a two way process, and the bioconjugate a one way process. FTIR measurements indicate an increase in the α-helical content of the protein and a change in the environment of the tryptophan residues that bury in the 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.