RESUMEN
CdTe quantum dots (QDs) were synthesized in aqueous solution using thioglycolic acid (TGA) as stabilizing agents. The interaction between TGA-CdTe QDs and fat mass and obesity-associated (FTO) protein was investigated by fluorescence, UV-visible absorption, synchronous fluorescence and three-dimensional fluorescence spectroscopy. Results revealed that TGA-CdTe QDs could strongly quench the intrinsic fluorescence of FTO protein with a static quenching procedure. Both the van der Waals and hydrogen bonding played a major role in stabilizing the complex. The binding constant and thermodynamic parameters at different temperatures were obtained. In addition, we found that the fluorescence intensity of QDs was significantly enhanced by the addition of FTO protein. Based on this, a sensitive method for detecting FTO protein was obtained in the linear range of 5.52×10(-9)-6.62×10(-7) mol L(-1) with the detection limit of 1.14×10(-9) mol L(-1). The influences of factors on the interaction between FTO protein and TGA-CdTe QDs were studied.
Asunto(s)
Compuestos de Cadmio/metabolismo , Proteínas/metabolismo , Puntos Cuánticos/metabolismo , Telurio/metabolismo , Tioglicolatos/metabolismo , Calibración , Cinética , Espectrometría de Fluorescencia , Espectrofotometría Ultravioleta , Temperatura , Factores de TiempoRESUMEN
The interactions between pepsin and four alkaloids, including caffeine (Caf), aminophylline (Ami), acefylline (Ace), diprophylline (Dip), were investigated by fluorescence, UV-visible absorption, resonance light scattering, synchronous fluorescence spectroscopy and 3D spectroscopy under mimic physiological conditions. The results revealed that Caf (Ami/Ace/Dip) caused the fluorescence quenching of pepsin by the formation of Caf (Ami/Ace/Dip)-pepsin complex. The binding constants and thermodynamic parameters at three different temperatures, the binding locality and the binding power were obtained. The hydrophobic and electrostatic interactions were the predominant intermolecular forces to stabilize the complex. Results showed that aminophylline was the stronger quencher and bound to pepsin with higher affinity than other three alkaloids.