Selective binding of uranyl cation by a novel calmodulin peptide

A 33-amino acid peptide corresponding to the helix-loop-helix motif of the calcium binding site I of the protein calmodulin from Paramecium Tetraurelia has been synthesized its binding properties with heavy metal ions have been studied. Herein, we demonstrate that two mutations of two aspartic acid...

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Bibliographic Details
Published inEnvironmental chemistry letters Vol. 4; no. 1; pp. 45 - 49
Main Authors Le Clainche, L, Vita, C
Format Journal Article
LanguageEnglish
Published Dordrecht Springer Nature B.V 01.04.2006
Subjects
Amino acids
Binding sites
Biosensors
Heavy metals
Paramecium tetraurelia
Peptides
Proteins
Uranium
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Summary:A 33-amino acid peptide corresponding to the helix-loop-helix motif of the calcium binding site I of the protein calmodulin from Paramecium Tetraurelia has been synthesized its binding properties with heavy metal ions have been studied. Herein, we demonstrate that two mutations of two aspartic acid residues in the peptide sequence gave access to a new peptide, which was selective for the uranyl ion UO^sub 2^ ^sup 2+^. This new peptide can be useful for the development of selective uranyl biosensors to monitor the presence of uranium in contaminated environments.[PUBLICATION ABSTRACT]
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ISSN:1610-3653
1610-3661
DOI:10.1007/s10311-005-0033-y