Structural Characterization of Zinc–Sucrose Complex and Its Ability to Promote Zinc Absorption in Caco-2 Monolayer Cells and Mice

Abstract

Sucrose emerges as a metal-ion chelating agent with excellent stability that may increase metal-ion absorption. This study aimed to characterize the structure of zinc−sucrose complex and investigate its ability to promote zinc absorption in Caco-2 monolayer cells and mice. Based on the results of the inductively coupled plasma emission spectrometer (ICP-ES), scanning electron microscopy−energy-dispersive X-ray spectroscopy (SEM-EDX), and Fourier transform infrared spectroscopy (FT-IR), it can be inferred that zinc and sucrose were chelated at a 1:1 ratio, with the hydroxyl groups playing a significant role. The Caco-2 monolayer cell model revealed that zinc−sucrose complex increased the amount of zinc uptake, retention, and transport in a dose-and timedependent manner. Through the upregulation of genes and proteins for ZIP4, MT1, and DMT1, treatment with zinc−sucrose complex improved the proportion of absorbed zinc utilized for transport compared to ZnCl 2 (26.21 ± 4.96 versus 8.50 ± 1.51%). Pharmacokinetic analysis of mice confirmed the zinc absorption-promoting effect of zinc−sucrose complex, as indicated by the considerably higher serum zinc level (4.16 ± 0.53 versus 2.56 ± 0.45 mg/L) and intestinal ZIP4, MT1, and DMT1 gene expression than ZnCl 2 . Further treatment of different zinc channel inhibitors and CETSA demonstrated the direct interaction of zinc−sucrose complex with ZIP4 protein and ZIP4-mediated cellular transport of zinc−sucrose complex. These findings provide a novel insight into the zinc absorption-promoting mechanism of zinc−sucrose complex, which could be used as an ingredient in functional foods to treat zinc deficiency.

Protective effect of vitexin against high fat-induced vascular endothelial inflammation through inhibiting trimethylamineN-oxide-mediated RNA m6A modification

“…RT-qPCR was performed with the ChamQ Universal SYBR qPCR master mix kit (Vazyme, Nanjing, China) as previously described. 21 The 10 μL reaction system consisted of 5 μL SYBR, 4.4 μL cDNA, 0.3 μL forward primer, and 0.3 μL reverse primer. The specific primers are listed in Table S2 †.…”