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Fluorescence spectroscopy of interaction between divalent lead ion and bovine serum albumin

Shuwei Li

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Abstract

The method of Fluorescence has studied the interaction between divalent lead ions and bovine serum albumin and has measured Pb2+ and BSA fluorescence spectra under different conditions,at the same time exploring the interacting mode of the two by thermodynamic calculations and BSA fluorescence quenching mechanism,Pb2+ and the binding constant between BSA and the binding site.The results show that,Pb2+ on the BSA fluorescence quenching is static quenching,Pb2+ into the BSA by hydrophobic forces to interact with the hydrophobic cavity,reaction △G=4.15 × 104 J·mol-1,△S=136 J/(mol·K),binding constant KA=2.07 × 107 L·mol-1,combined with the number of n=1.366.This simulates the impact of Pb2+ on the human body mechanism and provides the theoretical reference data For the Pb2+ in the toxicological analysis.

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What this paper is about

The method of Fluorescence has studied the interaction between divalent lead ions and bovine serum albumin and has measured Pb2+ and BSA fluorescence spectra under different conditions,at the same time exploring the interacting mode of the two by thermodynamic calculations and BSA fluorescence quenching mechanism,Pb2+ and the binding constant between BSA and the binding site.The results show that,Pb2+ on the BSA fluorescence quenching is static quenching,Pb2+ into the BSA by hydrophobic forces to interact with the hydrophobic cavity,reaction △G=4.15 × 104 J·mol-1,△S=136 J/(mol·K),binding constant KA=2.07 × 107 L·mol-1,combined with the number of n=1.366.This simulates the impact of Pb2+ on the human body mechanism and provides the theoretical reference data For the Pb2+ in the toxicological analysis.

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Available abstract

The method of Fluorescence has studied the interaction between divalent lead ions and bovine serum albumin and has measured Pb2+ and BSA fluorescence spectra under different conditions,at the same time exploring the interacting mode of the two by thermodynamic calculations and BSA fluorescence quenching mechanism,Pb2+ and the binding constant between BSA and the binding site.The results show that,Pb2+ on the BSA fluorescence quenching is static quenching,Pb2+ into the BSA by hydrophobic forces to interact with the hydrophobic cavity,reaction △G=4.15 × 104 J·mol-1,△S=136 J/(mol·K),binding constant KA=2.07 × 107 L·mol-1,combined with the number of n=1.366.This simulates the impact of Pb2+ on the human body mechanism and provides the theoretical reference data For the Pb2+ in the toxicological analysis.

Key concepts: Bovine serum albumin, Chemistry, Divalent, Quenching (fluorescence), Fluorescence, Binding constant, Fluorescence spectroscopy, Ion

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