Protein stabilization through supramolecular host–guest interactions with cyclodextrin-modified nanoparticles

Abstract

This study demonstrates the protein stabilization of gelatin through supramolecular interactions of silica nanoparticles and the influence on the point of denaturation. The phenomenon was studied in diluted solutions by dynamic light scattering, viscosity measurements, and differential scanning calorimetry. Native gelatin is stabilized by cyclodextrin functionalized SiO2 nanoparticles. After heating, increased supramolecular interactions of the nanoparticles with the denaturated gelatin coils are observed by progressive agglomeration. The described observation also resulted in a melting temperature shift from 30 °C, for native gelatin, to about 47 °C for the gelatin/CD-SiO2, which indicates the supramolecular stabilization of the gelatin chain structure. It was found that the gelatin is supramolecularly immobilized on the nanoparticle up to a certain temperature through complexation by cyclodextrin. The described results, also confirmed by DSC and viscosity measurements, show the prospect of using cyclodextrin-modified surfaces for the immobilization of the proteins.