Molecular interaction investigation between three CdTe:Zn2+ quantum dots and human serum albumin: A comparative study

Abstract

Water-soluble Zn-doped CdTe quantum dots (CdTe:Zn2+ QDs) have attracted great attention in biological and biomedical applications. In particular, for any potential in vivo application, the interaction of CdTe:Zn2+ QDs with human serum albumin (HSA) is of greatest importance. As a step toward the elucidation of the fate of CdTe:Zn2+ QDs introduced to organism, the molecular interactions between CdTe:Zn2+ QDs with three different sizes and HSA were systematically investigated by spectroscopic techniques. Three CdTe:Zn2+ QDs with maximum emission of 514nm (green QDs, GQDs), 578nm (yellow QDs, YQDs), and 640nm (red QDs, RQDs) were tested. The binding of CdTe:Zn2+ QDs with HSA was a result of the formation of HSA-QDs complex and electrostatic interactions played major roles in stabilizing the complex. The Stern–Volmer quenching constant, associative binding constant, and corresponding thermodynamic parameters were calculated. The site-specific probe competitive experiments revealed that the binding location of CdTe:Zn2+ QDs with HSA was around site I. The microenvironmental and conformational changes of HSA induced by CdTe:Zn2+ QDs were analyzed. These results suggested that the conformational change of HSA was dramatically at secondary structure level and the biological activity of HSA was weakened in the present of CdTe:Zn2+ QDs with bigger size.