Adsorption dynamics study on interactions of pigments and human whole saliva

Abstract

In situ, real timely and dynamically monitoring the processes of theaflavin (TF), curcumin (Cur) and cyanidin (Cy) binding to human whole saliva (WS) surface has been investigated by surface plasmon resonance (SPR) technique at the molecular level. The affinity between pigments and WS, association rate constant (k(a)), dissociation rate constant (k(d)), association equilibrium constant (K(A)) and dissociation equilibrium constant (K(D)) of pigments binding on WS surface had been determined by SPR and the Langmuir model as well as the Freundlich model. The data were analyzed by one-way ANOVA and SNK-q test. There were significant differences among TF, Cur and Cy in k(a), k(d), K(A) and K(D) (P<0.05). Our results showed that the adsorption isotherm of pigments on WS surface could be better described by the Freundlich model than the Langmuir model. The pigments adsorption on WS surface was dominant by specific interactions, such as hydrogen bonding. The affinity of pigments to WS were TF> Cur>Cy (P<0.05), as evidenced by the rate constants and equilibrium constants. Compared with Cur and Cy, TF shows much higher adsorption capacity on WS surface, suggesting the importance of the hydroxyl group in pigment/protein interactions.