Spectroscopic analysis on the binding interaction of biologically active pyrimidine derivative with bovine serum albumin.

Interactions between antimalarial indolone-N-oxide derivatives and human serum albumin.

Chiral recognition in separation science - an update.

Green synthesis of iron nanoparticles by various tea extracts: comparative study of the reactivity.

Tartrazine is an artificial azo dye commonly used in food products. The present study evaluated the interaction of tartrazine with two serum albumins (SAs), human serum albumin (HSA) and bovine serum albumin (BSA), under physiological conditions by means of fluorescence, three-dimensional fluorescence, UV-vis absorption, and circular dichroism (CD) techniques. The fluorescence data showed that tartrazine could bind to the two SAs to form a complex. The binding process was a spontaneous molecular interaction procedure, in which van der Waals and hydrogen bond interactions played a major role. Additionally, as shown by the UV-vis absorption, three-dimensional fluorescence, and CD results, tartrazine could lead to conformational and some microenvironmental changes of both SAs, which may affect the physiological functions of SAs. The work provides important insight into the mechanism of toxicity of tartrazine in vivo.

Characterizing the Interaction between Tartrazine and Two Serum Albumins by a Hybrid Spectroscopic Approach

Fluorescence spectroscopic investigation of the interaction between chloramphenicol and lysozyme

A study of the binding of C.I. Mordant Red 3 with bovine serum albumin using fluorescence spectroscopy

Characterization of Alizarin Red S binding sites and structural changes on human serum albumin: a biophysical study.

The binding of C.I. Acid Red 2 to human serum albumin: Determination of binding mechanism and binding site using fluorescence spectroscopy

Chloramphenicol binding to human serum albumin: Determination of binding constants and binding sites by steady-state fluorescence

Fei Ding

Papers

Fluorescence spectroscopic investigation of the interaction between chloramphenicol and lysozyme

A study of the binding of C.I. Mordant Red 3 with bovine serum albumin using fluorescence spectroscopy

Characterization of Alizarin Red S binding sites and structural changes on human serum albumin: a biophysical study.

The binding of C.I. Acid Red 2 to human serum albumin: Determination of binding mechanism and binding site using fluorescence spectroscopy

Chloramphenicol binding to human serum albumin: Determination of binding constants and binding sites by steady-state fluorescence