Model peptide studies of Ag+ binding sites from the silver resistance protein SilE

V. Chabert; M. Hologne; O. Sénèque; A. Crochet; O. Walker; K. M. Fromm

doi:10.1039/C7CC02630G

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Model peptide studies of Ag⁺ binding sites from the silver resistance protein SilE†

V. Chabert,

^a M. Hologne,

^b O. Sénèque,^c A. Crochet,

^d O. Walker

^b and K. M. Fromm

*^a

Author affiliations

* Corresponding authors

^a Univ. Fribourg, Department of Chemistry, Chemin du Musée 9, 1700 Fribourg, Switzerland
E-mail: katharina.fromm@unifr.ch

^b Univ. Lyon, CNRS, UCB Lyon 1, ENS-Lyon, Institut des Sciences Analytiques, UMR 5280, 5 rue de la Doua, 69100 Villeurbanne, France

^c Univ. Grenoble Alpes, CNRS, CEA, LCBM (UMR 5249), F-38000 Grenoble, France

^d Univ. Fribourg, Fribourg Center for Nanomaterials, FriMat, Chemin du Musée 9, 1700 Fribourg, Switzerland

Abstract

Using model peptides, each of the nine MX₂H or HX_nM (n = 1, 2) motifs of the silver resistance protein SilE has been shown to coordinate to one Ag⁺ ion by its histidine and methionine residues with K_d in the μM range. This suggests an Ag⁺ buffering role for SilE in the case of high Ag⁺ overload.

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Article information

DOI: https://doi.org/10.1039/C7CC02630G
Article type: Communication
Submitted: 05 Apr 2017
Accepted: 10 May 2017
First published: 11 May 2017

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Chem. Commun., 2017,53, 6105-6108

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Model peptide studies of Ag⁺ binding sites from the silver resistance protein SilE

V. Chabert, M. Hologne, O. Sénèque, A. Crochet, O. Walker and K. M. Fromm, Chem. Commun., 2017, 53, 6105 DOI: 10.1039/C7CC02630G

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