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Engineering Short Peptide Sequences for Uranyl Binding.
- Source :
-
Chemistry - A European Journal . Dec2014, Vol. 20 Issue 50, p16566-16573. 8p. - Publication Year :
- 2014
-
Abstract
- Peptides are interesting tools to rationalize uranyl-protein interactions, which are relevant to uranium toxicity in vivo. Structured cyclic peptide scaffolds were chosen as promising candidates to coordinate uranyl thanks to four amino acid side chains pre-oriented towards the dioxo cation equatorial plane. The binding of uranyl by a series of decapeptides has been investigated with complementary analytical and spectroscopic methods to determine the key parameters for the formation of stable uranyl-peptide complexes. The molar ellipticity of the uranyl complex at 195 nm is directly correlated to its stability, which demonstrates that the β-sheet structure is optimal for high stability in the peptide series. Cyclodecapeptides with four glutamate residues exhibit the highest affinities for uranyl with log KC=8.0-8.4 and, therefore, appear as good starting points for the design of high-affinity uranyl-chelating peptides. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09476539
- Volume :
- 20
- Issue :
- 50
- Database :
- Academic Search Index
- Journal :
- Chemistry - A European Journal
- Publication Type :
- Academic Journal
- Accession number :
- 99711582
- Full Text :
- https://doi.org/10.1002/chem.201404546