Thermodynamic Implications and Time Evolution of the Interactions of Near-Infrared PbS Quantum Dots with Human Serum Albumin
Qian Wang, Wenqi Chen, Xingyu Liu, Yi Liu, Feng‐Lei Jiang
Abstract
) indicated that the interaction resembled a protein-protein association. The both negative signs of enthalpy change and entropy change were elucidated by a proposed "two-step association-interaction" (TSAI) model. Agarose gel electrophoresis (AGE) and dynamic light scattering (DLS) showed that the binding ratio was roughly 2:1 (HSA/QDs), resembling sandwich-like structures. Furthermore, the secondary structure of HSA depended on the concentration of added QDs and the incubation time. The results preliminarily uncovered the physicochemical properties of QDs in the presence of proteins and elucidated the role of time evolution. These will inspire us to make the fluorescent QDs more biocompatible and use them in a proper way.