Study of protein coatings cross-linked via the free-radical mechanism on magnetic nanoparticles by the method of spectral and fluorescent probes

Abstract

Magnetite nanoparticles have been obtained with stable coatings formed from bovine and human serum albumins. The coatings are fixed by free-radical cross-linking of the proteins with the use of their ability to form interchain covalent bonds under the action of free radicals, which are generated with participation of transition metals present on nanoparticle surface. The method of spectral and fluorescent probes has been employed for the first time to describe the properties of coatings with the use of various dyes. It has been shown that, when studying the adsorption and free-radical cross-linking of proteins on nanoparticles, it is reasonable to use polymethine and squarylium dyes for estimating the functional properties of the proteins forming the coatings. It has been found that as many as 50% of molecules forming an albumin coating crosslinked via the free-radical mechanism retain their capability of bonding to a fluorescent dye. It has been concluded that the proteins occurring in the structure of the coatings retain their functional properties.