Le couplage CE-ICP/MS, un outil puissant pour la description des interactions protéine/métal

International audienc

Hyphenated capillary electrophoresis ICP/MS: a promising technique to boost the metallomics toolbox

International audienc

Interactions between copper (II) and β-amyloid peptide using capillary electrophoresis–ICP–MS: Kd measurements at the nanogram scale

International audienceAlthough the interaction between the β-amyloid peptide and copper (II) appears to play an important role in Alzheimer’s disease, the affinity constant is still controversial and values are ranging from 107 to 1011 M−1. With the aim of clarifying this point, a complementary method, based on the capillary electrophoresis–ICP–MS hyphenation, was developed and competitive binding experiments were conducted in the presence of nitrilotriacetic acid. The effect of the capillary surface (neutral or positively charged) and nature of the buffer (Tris or Hepes) have been studied. Tris buffer was found to be inappropriate for such determination as it enhances the dissociation of copper (II) complexes, already occurring in the presence of an electric field in capillary electrophoresis. Using Hepes, a value of 1010 M−1 was found for the affinity of the small β-amyloid peptide 1–16 for copper (II), which is in agreement with the values obtained for other proteins involved in neurodegenerative diseases. These constants were also determined in conditions closer to those of biological media (higher ionic strength, presence of carbonates)

CE-ICP/MS and TDA/ICP-MS for the characterization of a therapeutic gadolinium-based nanoparticle

International audienc

Hyphenated CE-ICP/MS : a promising technique to boost the metallomics toolbox

International audienc

Interactions protéine/métal : les potentialités du couplage CE-ICP/M

National audienc

Interactions protéine/métal : les potentialités du couplage CE-ICP/M

National audienc

A simple cladding process to apply monolithic silica rods in high performance liquid chromatography

International audienc

Separative techniques for metalloproteomics require balance between separation and perturbation

International audienceMetal-binding proteins play a crucial role in biological systems and associated metals display many critical functions, so many analytical tools have been developed to identify metal-protein complexes. However, identification of metal-protein complexes remains challenging since it addresses non-covalently bound species that may dissociate during analysis, due to their separation from their medium or to the interactions implicit in the separation. Many strategies, usually involving separation techniques coupled with elemental detection, have been investigated to overcome technical issues that hamper the identification and the characterization of metal-protein complexes. This review focuses on the separation techniques used in this field and their impact on dissociation of metal-protein complexes. We discuss metal losses induced by both the separation system and disequilibrium effects