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The aim of the study was to determine the efficacy of different products containing fluoride, calcium and phosphate for enamel remineralization in eroded primary teeth. A total of 90 sound primary canine teeth were randomly divided into 5 groups of 18 teeth each: 1) control (polished enamel), 2) 5% DuraShield sodium fluoride varnish, 3) 500 ppm fluoridated toothpaste, 4) casein phosphopeptide-amorphous calcium phosphate (CPP-ACP) cream, and 5) Clinpro White varnish containing functionalized tri-calcium phosphate (fTCP). Enamel microhardness (EMH) was measured in all samples before and after demineralization and after 28 days of remineralization. Also 8 samples in groups 2 to 5 and four samples of sound and demineralized enamel were examined with atomic force microscopy (AFM). All data were analyzed with one-way ANOVA (p<0.05). Mean microhardness of demineralized enamel was significantly lower than in enamel at baseline (p<0.001). Remineralization significantly increased microharness in groups 2 to 5 compared to the control group (p<0.001). Percent EMH after remineralization with CPP-ACP was significantly higher than after fTCP (p=0.029), toothpaste (p< 0.001) or fluoride varnish (p<0.001); however, there was no significant difference between toothpaste and fluoride varnish (p=0.062). Microhardness increased more after fTCP treatment than after treatment with sodium fluoride varnish (p<0.001) or fluoridated toothpaste (p=0.045). AFM images showed that enamel roughness decreased most after treatment with fTCP, followed by CPP-ACP, toothpaste and fluoride varnish. The efficacy of CPP-ACP cream for remineralizing eroded enamel was greater than fluoride toothpaste, fluoride varnish or fTCP varnish.

Modification of proteins by nonenzymatic glycation is one of the underlying factors that contribute to the development of the complications of diabetes. Human serum albumin (HSA) is one of the major targets of interaction with glucose through the Maillard reaction. The effects of 1 and 5 mg/ml glucose concentrations, which are consistent with blood glucose levels found in diabetic patients, on human serum albumin were studied by circular dichroism and fluorescence spectroscopy in sodium phosphate buffer, pH 7.4. Partial denaturation and changes in the structural integrity of HSA are caused by glycation at lower (1 mg/ml) and higher (5 mg/ml) concentrations of glucose. To study the relationship between structure and function, we investigated the interaction of L-tryptophan (L-Trp) with glycated and non-glycated HSA. The results showed that L-Trp, as the only free amino acid that substantially binds to HSA, has a lower affinity for the glycated form (especially at low concentrations of glucose) than for non-glycated HSA.

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