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Herein, a novel type of red-emitting carbon dots called TN-CDs was created via a one-step hydrothermal approach using neutral red and tartaric acid as raw materials. The fluorescence of TN-CDs was gradually quenched as the amount of water increased, and the color of the solution changed from yellow to pink mauve (or purple to pink). The reaction could be completed within only 5 s in various organic solvents such as N,N-Dimethylformamide (DMF), methanol (MeOH), acetonitrile (ACN), and ethanol (EtOH) with linear detection ranges of 1.2%-35.0%, 0.5%-20.0%, 0.25%-5.0% and 0%-16.0%, respectively. In addition, we prepared a reusable test strip and then combined it with TN-CDs to detect water content in DMF, as well as integrated it with smartphone software, a UV lamp, and a dark chamber for real-time, on-site, visual quantitative detection of the water content., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier B.V. All rights reserved.)

On the basis of fluorescence resonance energy transfer (FRET), a new rhodamine derivative (DRh) was synthesized as a ratiometric fluorescent probe for detecting Hg(2+) in water and living cells samples. The recognition properties of the probe DRh with metal ions had been investigated in H2O/CH3CN (9:1, v/v; Tris-HCl 50mmolL(-1); pH=7.0) solution by the UV-Vis spectrophotometry and the fluorescence spectrophotometry. The results showed that the probe DRh exhibited the selective recognition of Hg(2+). Upon the addition of Hg(2+), the spirolactam ring of probe DRh was opened. The 1:1 stoichiometric structure between DRh and Hg(2+) were supported by Job's plot, MS and DFT theoretical calculations. The linearly fluorescence intensity ratio (I582/I538) is proportional to the concentration of Hg(2+) in the range 0-30μmolL(-1). The limit of detection (LOD) of Hg(2+) is 0.008μmolL(-1) (base on S/N=3). The present probe was applied to the determination of Hg(2+) in neutral water samples and gave recoveries ranging from 104.5 to 107.9%. Furthermore, the fluorescent probe also can be applied as a bioimaging reagent for Hg(2+) detection in HeLa cells., (Copyright © 2016 Elsevier B.V. All rights reserved.)

The resonance light scattering (RLS) spectra of bovine serum albumin (BSA)-dithiothreitol (DTT)-sodium dodecylbenzene sulphonate (SDBS) and its analytical application were investigated. The RLS intensity of this system can be effectively enhanced in the presence of BSA. Based on the enhanced RLS intensity, a simple assay for BSA was developed. The experimental results indicate that the enhanced RLS intensity is proportional to the concentration of BSA in the range from 1.0 x 10(-8) to 7.5 x 10(-7) mol L(-1) with the determination limit of 5.0 x 10(-9) mol L(-1). The effects of pH, concentration of SDBS and DTT on the RLS enhancement were discussed. Most metal ions have little interference on the determination of BSA. Some synthetic and real samples were analyzed, and the results obtained were in good agreement with those obtained by Bradford method.

In this paper, the anionic surfactant sodium dodecylbenzene sulphonate (SDBS) and cationic surfactant cetyltrimethylammonium bromide (CTMAB) were used as resonance light scattering (RLS) probe to determine bovine serum albumin (BSA). Based on the weak RLS intensity of SDBS-CTMAB probe and the enhancement of RLS intensity of BSA in the presence of the probe, a simple assay for BSA was developed. The experimental results showed that the formation of three component complex BSA-SDBS-CTMAB is the main reason for the enhancement of RLS intensity of BSA, in which SDBS as a bridge can interact with both BSA and CTMAB. The effects of pH value, incubation time, concentrations of SDBS and CTMAB on the enhanced RLS intensity of BSA were investigated. Under the optimum conditions, the enhanced RLS intensity is proportional to the concentration of BSA in the range from 2.5 x 10(-8) to 2.0 x 10(-6)mol L(-1). The detection limit is 9.7 x 10(-9) mol L(-1) for BSA. The study of foreign substance effect on the determination of BSA indicated that most of metal ions have little effect on the determination of BSA. The results of assay for BSA in synthetic samples were satisfactory.

As a resonance light scattering (RLS) probe, the polyelectrolyte polymethacrylic acid (PMAA) was applied in this assay. The bovine serum albumin (BSA) and human serum albumin (HSA) were determined by the electrostatic interaction of PMAA and proteins. At pH 3.8 Na(2)HPO(4)-citric acid buffer solution, the RLS intensities of PMAA-BSA (HSA) system were greatly enhanced. The characteristic peaks were appeared at the wavelength 320, 546 and 594 nm. The optimization conditions of the reaction were also examined and selected. Under the selected conditions, the RLS intensities were proportional to the protein concentrations in the range of (0.0200-2.00) x 10(-6) mol/L for BSA and (0.0200-2.40) x 10(-6) mol/L for HSA. The influences of some foreign substances were also examined. The synthetic samples containing proteins and some real samples were analyzed and the results obtained were satisfactory.

By means of the resonance light scattering (RLS) technique, a new method was developed to determine the bovine serum albumin (BSA) and human serum albumin (HSA) by the interaction of serum albumin with poly(diallyldimethylammonium chloride) (PDDA). At Tris-NaOH buffer solution, the RLS intensity of serum albumin at the wavelength 320, 550 and 590 nm was obviously enhanced in the presence of PDDA. The influences of some experimental factors, including incubation time, addition sequence of reagents, pH value, concentration of PDDA and foreign substances, on the enhancement of the RLS intensity were examined. The optimum conditions of the experiment were selected. Under the selected experimental condition, the enhanced RLS intensities were directly proportional to the concentrations in the range of (0.0250-2.75)x10(-6) mol/L for BSA and (0.0235-1.17)x10(-6) mol/L for HSA. The detection limits (S/N=3) were 8.40x10(-9) mol/L for BSA and 7.39x10(-9) mol/L for HSA. The synthetic samples were analysed and the results obtained were satisfactory.

A simple, highly sensitive assay for fibronectin (Fn) was reported using resonance light-scattering (RLS) technique based on the enhanced RLS intensity of hyperin-cetyltrimethylammonium bromide (CTMAB)-Fn system. The interaction system of hyperin-CTMAB-Fn was investigated using spectral methods. Mechanistic investigations show that the main reason of the enhanced RLS intensity of Fn is the formation of three-component complex (hyperin-CTMAB-Fn), in which CTMAB acts as a bridge between hyperin and Fn. The effects of pH, surfactant, concentration of CTMAB and hyperin, incubation time and foreign substances on the enhancement of RLS intensity were studied. Under the optimum conditions, the enhancement of RLS intensity is in proportion to the concentration of Fn in the range of 1.9-248ng/ml. The synthetic samples containing Fn were analyzed and results obtained were satisfied.

Based on the interaction between human complement factor C4 (human C4) and sodium dodecylbenzene sulphonate (SDBS) and the resonance light-scattering (RLS) technique, a highly sensitive assay for human C4 using resonance light-scattering technique was developed. At pH 2.8 Na2HPO4-citric acid buffer solution, the RLS intensities of SDBS system at 283, 503 and 600 nm were obviously enhanced in the presence of human C4. The effects of surfactant, pH, incubation time, concentration of SDBS and foreign substances on the enhanced RLS intensity of system were investigated. Under the optimum conditions, the enhanced RLS intensity is directly proportional to the concentration of human C4 in the range of (0.5-120)x10(-6)gl-1 and the linear regression equation was obtained with high correlation coefficient. This RLS technique was applied to the determination of human C4 in some synthetic samples with good recovery. Moreover, it was found that the electrostatic interaction is the main binding force between SDBS and human C4.

The interactions of colloidal gold and serum albumins, including bovine serum albumin (BSA) and human serum albumin (HSA), were studied by fluorescence and absorption spectrometry. Fluorescence quenching spectrometry was applied to study the interactions between colloidal gold and serum albumins. At pH 7.4 phosphate-buffered saline (PBS), the intensity of fluorescence emission spectrum of serum albumins decreased in the presence of colloidal gold, which indicated that colloidal gold quenched the fluorescence of serum albumins. Experimental results indicated that the combination reactions of colloidal gold and serum albumins were static quenching processes. Based on the effect of colloidal gold on fluorescence intensity, the binding constants, the numbers of binding sites and the acting forces between colloidal gold and serum albumins were found.