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

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.

[1]  J. Schwartz,et al.  Relationship between childhood blood lead levels and stature. , 1986, Pediatrics.

[2]  R. Stauber,et al.  Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties , 2007, British journal of pharmacology.

[3]  H. Jakubowski,et al.  Cross-talk between Cys34 and Lysine Residues in Human Serum Albumin Revealed by N-Homocysteinylation* , 2004, Journal of Biological Chemistry.

[4]  L. Peng,et al.  Calorimetric Study of Nonspecific Interaction Between Lead Ions and Bovine Serum Albumin , 2007, Biological Trace Element Research.

[5]  A. Tappel,et al.  Fluorescent modification of serum albumin by lipid peroxidation , 1971, Lipids.

[6]  S. Curry Beyond Expansion: Structural Studies on the Transport Roles of Human Serum Albumin , 2002, Vox sanguinis.

[7]  F. J. Holler,et al.  Principles of Instrumental Analysis , 1973 .

[8]  D. Carter,et al.  Atomic structure and chemistry of human serum albumin , 1992, Nature.

[9]  G. Goldstein,et al.  Picomolar concentrations of lead stimulate brain protein kinase C , 1988, Nature.

[10]  J. Lakowicz,et al.  Tryptophan fluorescence intensity and anisotropy decays of human serum albumin resulting from one-photon and two-photon excitation. , 1992, Biophysical chemistry.

[11]  A. Feofanov,et al.  Camptothecin‐binding site in human serum albumin and protein transformations induced by drug binding , 1997, FEBS letters.

[12]  Andres F. Zuluaga,et al.  Fluorescence Excitation Emission Matrices of Human Tissue: A System for in vivo Measurement and Method of Data Analysis , 1999 .

[13]  S. Yao,et al.  Piezoelectric Quartz Crystal Impedance Study of the Pb^2+-induced Precipitation of Bovine Serum Albumin and Its Dissolution with EDTA in an Aqueous Solution , 2002, Analytical sciences : the international journal of the Japan Society for Analytical Chemistry.

[14]  Karl S Booksh,et al.  Excitation-emission matrix fluorescence spectroscopy in conjunction with multiway analysis for PAH detection in complex matrices. , 2006, The Analyst.

[15]  S. Curry,et al.  Crystal Structure Analysis of Warfarin Binding to Human Serum Albumin , 2001, The Journal of Biological Chemistry.

[16]  R. Hegele,et al.  Restriction isotyping of the premature termination variant of lipoprotein lipase in Alberta Hutterites. , 1996, Clinical biochemistry.

[17]  P. Goering Lead-protein interactions as a basis for lead toxicity. , 1993, Neurotoxicology.

[18]  Jing Li,et al.  A highly sensitive and selective catalytic DNA biosensor for lead ions [9] , 2000 .

[19]  R. Swaminathan,et al.  Novel Absorption and Fluorescence Characteristics of L-Lysine. , 2001 .