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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Published in: | Environmental chemistry letters Vol. 4; no. 1; pp. 45 - 49 |
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Main Authors: | , |
Format: | Journal Article |
Language: | English |
Published: |
Dordrecht
Springer Nature B.V
01-04-2006
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Subjects: | |
Online Access: | Get full text |
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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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1610-3653 1610-3661 |
DOI: | 10.1007/s10311-005-0033-y |