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• W2093809445 abstract "Studying metal–biomolecule interactions is critical to the elucidation of the molecular basis of the biological functions and toxicity of metals. In the present study, a competitive fluorimetric approach has been developed to measure the apparent affinity of biomolecules for Be2+ by using a Be2+-specific fluorigenic probe (10-hydroxybenzo[h]quinoline-7-sulfonate, HBQS). Under physiological conditions, HBQS coordinates with Be2+ in a molar ratio of 1:1 and results in a fluorescence shift from 580 nm for HBQS to 480 nm for the Be–HBQS complex associated with significant fluorescence enhancement. When a beryllium ligand is present in the mixture of Be2+ and HBQS, the competition of ligand against HBQS for beryllium ion binding results in dissociation and thus a fluorescence decrease of the Be–HBQS complex. By titrating ligand and monitoring the dose-dependent decrease of Be–HBQS complex fluorescence at 480 nm, the apparent affinity between ligand and Be2+ can be derived. Applying this simple approach, the apparent affinities of various nucleotides and the iron-storage protein ferritin for beryllium ion have been determined. In particular, the apparent dissociation constant of Be2+ and adenosine 5′-triphosphate (ATP) was also validated by an electrospray ionization mass spectrometric (ESI-MS) method. The general applicability of the proposed competition assay was further demonstrated using FluoZin-1, a zinc fluorescent indicator, in a binding study for Zn2+ and bovine serum albumin. This newly developed competitive fluorimetric assay provides a sensitive, simple, and generic approach for affinity estimation of metal and biomolecule binding." @default.
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• W2093809445 date "2011-07-01" @default.
• W2093809445 modified "2023-09-23" @default.
• W2093809445 title "Analysis of beryllium to biomolecule binding using a metal specific fluorescent probe and competitive assay" @default.
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• W2093809445 doi "https://doi.org/10.1016/j.talanta.2011.04.037" @default.
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