Characterization of water solubility and binding of spin labeled drugs in the presence of albumin nanoparticles and proteins by electron paramagnetic resonance spectroscopy

Abstract

Electron paramagnetic resonance (EPR) spectroscopy is an advantageous technique to monitor solubility of drugs in an aqueous solution. In the presence of a drug carrier, the bound and unbound drug fractions can be determined in the same sample simultaneously. To enhance the solubility of hydrophobic drugs, a transporter protein of bovine serum albumin (BSA) can be used directly or in the form of nanoparticle. Moreover, a cationic BSA can be used to enhance anionic drug loading. Here, drugs with different water solubility, salicylic acid (high), ibuprofen (low) and chlorambucil (none) were spin labeled and studied with EPR spectroscopy. Remarkably, it has been shown that albumin nanoparticles are much more effective than albumin proteins in dissolving hydrophobic drugs in water. Furthermore, different drug loading methods were compared, and different from other techniques drug release can be monitored directly from the NPs pellet dissolution by EPR spectroscopy.