Modification of proteins with cyclodextrins prevents aggregation and surface adsorption and increases thermal stability.

ABSTRACT

This work describes a general approach for preventing protein aggregation and surface adsorption by modifying proteins with ß-cyclodextrins (ßCD) via an efficient water-driven ligation. As compared to native unmodified proteins, the cyclodextrin-modified proteins (lysozyme and RNase A) exhibit significant reduction in aggregation, surface adsorption and increase in thermal stability. These results reveal a new chemistry for preventing protein aggregation and surface adsorption that is likely of different mechanisms than that by modifying proteins with poly(ethylene glycol).