Magnetic γ-Fe2O3 nanoparticles coated with poly-L-cysteine for chelation of As(III), Cu(II), Cd(II), Ni(II), Pb(II) and Zn(II)

Poly-l-cysteine (PLCysn) (n = 20) was immobilized onto the surface of commercially available magnetic gamma-Fe2O3 nanoparticles, and its use as a selective heavy metal chelator was demonstrated. Magnetic nanoparticles are an ideal support because they have a large surface area and can easily be retr...

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Veröffentlicht in:Journal of hazardous materials 2009-01, Vol.161 (2-3), p.848-853
Hauptverfasser: WHITE, Brianna R, STACKHOUSE, Brandon T, HOLCOMBE, James A
Format: Artikel
Sprache:eng
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Zusammenfassung:Poly-l-cysteine (PLCysn) (n = 20) was immobilized onto the surface of commercially available magnetic gamma-Fe2O3 nanoparticles, and its use as a selective heavy metal chelator was demonstrated. Magnetic nanoparticles are an ideal support because they have a large surface area and can easily be retrieved from an aqueous solution. PLCysn functionalization was confirmed using FTIR and the quantitative Ellman's test. Metal binding capacities for As(III), Cd(II), Cu(II), Ni(II), Pb(II) and Zn(II) were determined at pH 7.0 and compared to adsorption capacities for unfunctionalized gamma-Fe2O3 nanoparticles. The effect of pH on the PLCysn functionalized nanoparticles was also investigated. For all of the metals examined, binding capacities (mumol metal/g support) were more than an order of magnitude higher than those obtained for PLCysn on traditional supports. For As(III), Cu(II), Ni(II) and Zn(II), the binding capacities were also higher than the metal adsorption capacities of the unfunctionalized particles. Metal uptake was determined to be rapid ( < 2.5 min) and metal recoveries of > 50% were obtained for all of the metals except As(III). PLCysn, which has a general metal selectivity towards soft metals acids, was chosen to demonstrate the proof of concept. Greater metal selectivity may be achievable through the use of combinatorial peptide library screening or by using peptide fragments based on known metal binding proteins.
ISSN:0304-3894
1873-3336
DOI:10.1016/j.jhazmat.2008.04.105