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Updated: Jul 5, 2026

A Rapid and Quantitative Fluorimetric Method for Protein-Targeting Small Molecule Drug Screening
Published on: October 16, 2015
[Study on the interaction of serum albumin and micromolecule compounds by modified fluorescence spectra]
Rui Huang1, Zhi-Ning Xia, Ping Gong
1College of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400044, China. huangrui222@yahoo.com.cn
Abstract:
The fluorescence spectroscopy is widely used in the analysis of the interaction between serum albumin (SA) and micromolecule compound, in which SA is measured as the fluorescence source to provide interaction information. A modified method has been compared with the classical method in the present paper, where the micromolecule compounds were used as the interested analytes whose fluorescence spectra were measured. The binding constants obtained based on the classical and modified methods were found much different by studying the two systems, BSA-TX and BSA-SH. The result shows that the classical method has the drawback of taking the fluorescence source of tryptophan instead of all other amino acids groups in SA molecule. Two novel methods were then reported, namely the modified fluorescence spectrometry method and fluorescence background subtracting method. The former could reflect the whole information of the interaction system, while the latter effectively over-came the overlay of spectra in the system, where the fluorescence spectra of the two components interfere with each other terribly. The effectivity of the two novel methods has been proved by ultra-violet spectrometry.
