Interactions of hydrophobically modified hyaluronan carrier with bovine serum albumin

Abstract

The interactions of carrier systems with serum proteins complicate their performance in medical applications. Although interactions of proteins with native hyaluronan (HA) have been investigated, there is little known about the interactions of its derivatives. The interactions of the oleyl derivative of HA (oleyl-HA) with bovine serum albumin (BSA) were investigated using various physicochemical techniques to understand processes and structural changes at the molecular level. The response of used techniques could be divided into three regimes according to an interplay of hydrogen bonding, electrostatic, and hydrophobic interactions at certain BSA to oleyl-HA molar ratios. The hydrophobic interactions led to the incorporation of BSA into the carriers' structure resulting the formation of hybrid BSA-oleyl-HA nanostructures with increased curcumin loading. The structural changes were correlated with skin penetration experiments, which showed decreased penetration efficiency due to altered interfacial behavior of the hybrid nanostructures. The oleyl-HA carriers' ability to carry significant amounts of a hydrophobic active compound was preserved at both low and high amounts of BSA. The results provided important information about the complex behavior of hydrophobically modified HA derivatives in a biological environment. Acquired findings could accelerate the implementation of HA derivatives as drug delivery systems.