Carbon Dots Modified Multi Dopants Nitrogen and Boron for an Early Detection of Lead in the Environment.

The remarkable optical properties and strong biocompatibility of carbon dots make them highly promising for applications in biochemical sensing and environmental testing. These carbon dots possess a surface that is easily modifiable. In this study, carbon dots have been successfully synthesized and modified by the addition of N and B dopants using the microwave method, along with the functionalization of their surface functional groups with bovine serum albumin (BSA). The maximum fluorescence intensity of N, B-CDs is observed at 462 nm when excited at a wavelength of 352 nm. N, B-CDs have a spherical size with a diameter ranging from 2 to 6 nm, confirmed by UV-Vis absorption spectra and the presence of functional groups in the FT-IR absorption patterns. BSA-functionalized N, B-CDs as the fluorescent probe demonstrate great potential as a sensor for Pb(II) ions in water, with a very low detection limit of 1.05 µg/L. This research could contribute to the development of fluorescence nanosensors.

Long-term precision in capillary isoelectric focusing for protein analysis.

In order to improve precision in protein analysis, a new rinsing procedure with 3M hydrochloric acid was investigated for linear polyacrylamide-coated capillaries used in isoelectric focusing. After each run the capillaries were rinsed with hydrochloric acid for 5 min, followed by water for 20 min (Deltap = 1030 mbar each). Myoglobin, beta-lactoglobulin, and ovalbumin were used as model proteins; the pH gradient was provided by Pharmalyte (pH 3-10). The resulting method was already successful in avoiding capillary blockages, even for long-series protein measurements. Further improvements in precision have been obtained by avoiding a complete standstill of liquid within the capillary when the separation system was idle. Pressure (Deltap = 300 mbar or more) and high voltage (30 kV) were therefore also applied during storage within a measurement series. The reproducibility of migration time and peak area are further improved with RSD% less than 10% in a long-term measurement (n = 86).

Reproducible protein analysis by CE using linear polyacrylamide-coated capillaries and hydrochloric acid rinsing.

Hydrochloric acid was investigated as a rinsing reagent to remove adsorbed proteins from linear polyacrylamide-coated capillaries for electrophoresis. Three model proteins were used, namely cytochrome c as a basic protein, beta-lactoglobulin as an acidic protein, and beta-casein as a more easily denaturing protein. In order to regenerate capillary surfaces, they have been rinsed for 5 min with 2 M hydrochloric acid, 5 min with water, and then 30 min with buffer after every tenth run. It was found important to perform this regeneration procedure on time. The obtained results show good repeatability of the apparent EOF mobility with percentage RSDs below 3% (n = 60) in various cases. These good results were mainly confirmed in long-term series with more than 200 runs each. Only very high concentrations (175 microM) of beta-lactoglobulin and beta-casein at pH 3.5 gave RSD% values above 5%. For these conditions, the further test of 85% m/m phosphoric acid as rinsing reagent showed a good repeatability of the apparent EOF mobilities as well.