Determination of albumins by its quenching effect on the fluorescence of Tb3+-oxolinic acid complex in presence of sodium dodecyl sulphate

Wu, Xia; Zheng, Jinhua; Guo, Chengxiang; Yang, Jinghe; Ding, Honghong; Hu, Zhiyong; Li, Chao

doi:10.1016/j.jlumin.2006.06.011

Cited by 9 publications

(1 citation statement)

References 16 publications

(12 reference statements)

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“…After optimizing the experimental conditions to obtain maximum fluorescence enhancement, the calibration graphs were plotted using the data obtained by titrating BSA/HSA with 21 / 22 (SI Figures S1 and S2), and the results are documented in SI Tables S3 and S4. − The high sensitivity and efficiency of these newly developed probes encouraged us to investigate their potential in quantifying serum albumin present in blood serum. The detail of this quantification process has been provided in SI (Figure S16, Tables S5–S7).…”

Section: Resultsmentioning

confidence: 99%

Functional Molecular Lumino-Materials to Probe Serum Albumins: Solid Phase Selective Staining Through Noncovalent Fluorescent Labeling

Dey

Gupta

Mukherjee

et al. 2014

ACS Appl. Mater. Interfaces

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Selective staining of human serum albumin protein in gel electrophoresis over wide range of other protein(s) is extremely important because it contains more than 60% volume of serum fluid in human body. Given the nonexistence of suitable dye materials for selective staining of serum albumins in gel electrophoresis, we report a new class of easy synthesizable and low molecular weight staining agents based on 3-amino-N-alkyl-carbazole scaffold for selective staining of serum albumins in solid phase. A detailed structure-efficiency relationship (SER) study enabled us to develop two such potent functional molecular probes which stain both human and bovine serum albumin selectively in gel electrophoresis in the presence of other proteins and enzymes. The present gel staining process was found to be very simple and less time-consuming as compared to the conventional coomassie blue staining which in turn makes these probes a new class of serum albumin-specific staining materials in proteome research. Moreover, these molecular lumino-materials can detect serum albumins at subnanomolar level in the presence of broad spectrum of other proteins/enzymes in aqueous buffer (99.9% water, pH = 7.3) keeping the protein secondary structure intact. Our experimental and the docking simulation results show that these probes bind preferentially at 'binding site I' of both the serum proteins.

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