1. Engineering Short Peptide Sequences for Uranyl Binding.
- Author
-
Lebrun, Colette, Starck, Matthieu, Gathu, Vicky, Chenavier, Yves, and Delangle, Pascale
- Subjects
AMINO acid sequence ,AMINO acid analysis ,METAL scaffolding ,URANYL compounds synthesis ,URANIUM compounds synthesis - 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 K
C =8.0-8.4 and, therefore, appear as good starting points for the design of high-affinity uranyl-chelating peptides. [ABSTRACT FROM AUTHOR]- Published
- 2014
- Full Text
- View/download PDF