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Literature DB >> 19902002

Detection of picomolar concentrations of lead in water using albumin-based fluorescence sensor.

Abstract

Comprehensive analysis of fluorescence of albumin shows a weak fluorescence band at 430 nm, whose intensity exhibits a remarkable sensitivity to the presence of heavy ions in water. Using this fluorescence as a marker, as low as 10 pM concentration of lead can be routinely detected. Such a great sensitivity is explained in terms of electrostatic interactions in solution, which promote protein agglomeration. The latter is independently confirmed using dynamic light scattering measurements.

Entities: Chemical

Year: 2009 PMID： 19902002 PMCID： PMC2774347 DOI： 10.1063/1.3246792

Source DB: PubMed Journal: Appl Phys Lett ISSN： 0003-6951 Impact factor: 3.791

16 in total

1. Camptothecin-binding site in human serum albumin and protein transformations induced by drug binding.

Authors: F Fleury; A Ianoul; M Berjot; A Feofanov; A J Alix; I Nabiev
Journal: FEBS Lett Date: 1997-07-14 Impact factor: 4.124

2. Atomic structure and chemistry of human serum albumin.

Authors: X M He; D C Carter
Journal: Nature Date: 1992-07-16 Impact factor: 49.962

Review 3. Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties.

Authors: K Oettl; R E Stauber
Journal: Br J Pharmacol Date: 2007-04-30 Impact factor: 8.739

4. Picomolar concentrations of lead stimulate brain protein kinase C.

Authors: J Markovac; G W Goldstein
Journal: Nature Date: 1988-07-07 Impact factor: 49.962

5. Fluorescent modification of serum albumin by lipid peroxidation.

Authors: B L Fletcher; A L Tappel
Journal: Lipids Date: 1971-03 Impact factor: 1.880

6. Excitation-emission matrix fluorescence spectroscopy in conjunction with multiway analysis for PAH detection in complex matrices.

Authors: Michelle L Nahorniak; Karl S Booksh
Journal: Analyst Date: 2006-09-19 Impact factor: 4.616

7. Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I.

Authors: I Petitpas; A A Bhattacharya; S Twine; M East; S Curry
Journal: J Biol Chem Date: 2001-04-02 Impact factor: 5.157

8. Tryptophan fluorescence intensity and anisotropy decays of human serum albumin resulting from one-photon and two-photon excitation.

Authors: J R Lakowicz; I Gryczynski
Journal: Biophys Chem Date: 1992-11 Impact factor: 2.352

Detection of picomolar concentrations of lead in water using albumin-based fluorescence sensor.

1. Camptothecin-binding site in human serum albumin and protein transformations induced by drug binding.

2. Atomic structure and chemistry of human serum albumin.

Review 3. Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties.

4. Picomolar concentrations of lead stimulate brain protein kinase C.

5. Fluorescent modification of serum albumin by lipid peroxidation.

6. Excitation-emission matrix fluorescence spectroscopy in conjunction with multiway analysis for PAH detection in complex matrices.

7. Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I.

8. Tryptophan fluorescence intensity and anisotropy decays of human serum albumin resulting from one-photon and two-photon excitation.

9. Cross-talk between Cys34 and lysine residues in human serum albumin revealed by N-homocysteinylation.

Review 10. Lead-protein interactions as a basis for lead toxicity.

1. Structural changes of human serum albumin in response to a low concentration of heavy ions.

2. Raman spectroscopy provides a powerful diagnostic tool for accurate determination of albumin glycation.