ABSTRACT
To explore in vivo application of quantum dots (QDs), it is essential to understand the dynamics and energetics of interactions between QDs and proteins. Here, surface plasmon resonance (SPR) and molecular docking were employed to investigate the kinetics and thermodynamics of interactions between human serum albumin (HSA) and CdTe QDs (~3 nm) functionalized with mercaptopropionic acid (MPA) or thioglycolic acid (TGA). Kinetic analysis showed that HSA-QD interactions involved transition-complex formation. Despite the structural similarities between MPA and TGA, the [HSA-CdTe@TGA] formation by association of free HSA and QDs demanded 70% more energy and higher entropic gain (Ea-TGA= 65.10 and T∆Sa-TGA= 28.62 kJ mol-1) than the formation of [HSA-CdTe@MPA] (Ea-MPA = 38.13 and T∆Sa-MPA = 0.53kJ mol-1). While the [HSA-CdTe@MPA]° dissociation required higher energy and lower entropy loss (Ed-MPA = 49.96 and T∆Sd-MPA = - 32.18kJ mol-1) than the [HSA-CdTe@TGA]° dissociation (Ed-TGA= 30.78 and T∆Sd-TGA= - 51.12 kJ mol-1). The stability of [HSA-QDs]° was independent of the temperature and functionalizing group. However, the enthalpic and entropic components were highly affected by the substitution of MPA (ΔH° = - 11.83 and TΔS° = 32.72 kJ mol-1) with TGA (ΔH° = 34.31 and TΔS° = 79.73 kJ mol-1). Furthermore, molecular docking results indicated that the metal site on the QDs contributes to the stabilization of [HSA-QDs]°. Therefore, differences in QD functionalization and surface coverage densities can alter the HSA-QD interaction, thus their application.