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2011•Chinese Journal of Spectroscopy LaboratoryRequires access

Fluorescence Spectrometry for Interaction of [Zn(Phen)(5-Fu)_2](NO_3)_2 and Bovine Serum Albumin

Du Wu

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Abstract

A complex of [Zn(Phen)(5-Fu)2](NO3)2 was synthesized using Zn(NO3)2,fluorouracil(5-Fu),1,10-phenanthrotine(Phen) as starting materials.The interaction of [Zn(Phen)(5-Fu)2](NO3)2 with bovine serum albumin was studied by fluorescence spectrometry.The results showed that these interactions resulted in the endogenous fluorescence quenching of bovine serum albumin,which belonged to a static quenching mechanism.The binding constant Ka was 1.56×106L·mol-1 and the binding site n was 1.40.Moreover,the complex could quench 94.0% tryptophane(Trp) group in the bovine serum albumin surface,which would be an excellent quenching reagent in the future.

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What this paper is about

A complex of [Zn(Phen)(5-Fu)2](NO3)2 was synthesized using Zn(NO3)2,fluorouracil(5-Fu),1,10-phenanthrotine(Phen) as starting materials.The interaction of [Zn(Phen)(5-Fu)2](NO3)2 with bovine serum albumin was studied by fluorescence spectrometry.The results showed that these interactions resulted in the endogenous fluorescence quenching of bovine serum albumin,which belonged to a static quenching mechanism.The binding constant Ka was 1.56×106L·mol-1 and the binding site n was 1.40.Moreover,the complex could quench 94.0% tryptophane(Trp) group in the bovine serum albumin surface,which would be an excellent quenching reagent in the future.

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Available abstract

A complex of [Zn(Phen)(5-Fu)2](NO3)2 was synthesized using Zn(NO3)2,fluorouracil(5-Fu),1,10-phenanthrotine(Phen) as starting materials.The interaction of [Zn(Phen)(5-Fu)2](NO3)2 with bovine serum albumin was studied by fluorescence spectrometry.The results showed that these interactions resulted in the endogenous fluorescence quenching of bovine serum albumin,which belonged to a static quenching mechanism.The binding constant Ka was 1.56×106L·mol-1 and the binding site n was 1.40.Moreover,the complex could quench 94.0% tryptophane(Trp) group in the bovine serum albumin surface,which would be an excellent quenching reagent in the future.

Key concepts: Bovine serum albumin, Chemistry, Quenching (fluorescence), Fluorescence, Reagent, Binding constant, Serum albumin, Mass spectrometry

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Fluorescence Spectrometry for Interaction of [Zn(Phen)(5-Fu)_2](NO_3)_2 and Bovine Serum Albumin — Research Paper | ScholarLens