Biomimetic interactions of proteins with functionalized cadmium sulfide quantum dots

Abstract

Interactions between various modified semiconductor nanocrystal, cadmium sulfide quantum dots (CdS QDs) and bovine serum albumin (BSA) and lysozyme (LZY) were investigated. CdS QDs capped with mercaptoethanol (MPA), l-cysteine (Lcys) and glutathione (GSH) were synthesized in aqueous solution and characterized by UV–vis and fluorescence spectrum. Circular dichroism (CD) and fluorescence spectrum were used to detect the interactions between as-prepared CdS QDs and protein molecules. The interaction parameters, including binding constant ( K b ), binding site number ( n) and quench constant ( K q ), were determined by fluorescence spectrum. The changes of secondary structures of the proteins were detected by CD. The results imply that CdS QDs modified by different agents have dramatically different binding strength with protein molecules. The results obtained here analyze the biosafety of CdS QDs in terms of the biological behavior of biomolecules and could serve as basis for the application of CdS QDs to bioscience.