Importance of Post-translational Modifications in the Interaction of Proteins with Mineral Surfaces: The Case of Arginine Methylation and Silica surfaces - Archive ouverte HAL Access content directly
Journal Articles Langmuir Year : 2018

Importance of Post-translational Modifications in the Interaction of Proteins with Mineral Surfaces: The Case of Arginine Methylation and Silica surfaces

(1, 2) , (2) , (1) , (1) , (1, 2) , (1) , (1) , (3) , (2) , (1) , (1)
1
2
3

Abstract

Understanding the mechanisms involved in the interaction of proteins with inorganic surfaces is of major interest for both basic research and practical applications involving nanotechnology. From the list of cellular proteins with the highest affinity for silica nanoparticles, we highlighted the group of proteins containing arginine–glycine–glycine (RGG) motifs. Biochemical experiments confirmed that RGG motifs interact strongly with the silica surfaces. The affinity of these motifs is further increased when the R residue is asymmetrically, but not symmetrically, dimethylated. Molecular dynamics simulations show that the asymmetrical dimethylation generates an electrostatic asymmetry in the guanidinium group of the R residue, orientating and stabilizing it on the silica surface. The RGG motifs (methylated or not) systematically target the siloxide groups on the silica surface through an ionic interaction, immediately strengthened by hydrogen bonds with proximal silanol and siloxane groups. Given that, in vivo, RGG motifs are often asymmetrically dimethylated by specific cellular methylases, our data add support to the idea that this type of methylation is a key mechanism for cells to regulate the interaction of the RGG proteins with their cellular partners.
Not file

Dates and versions

cea-01858455 , version 1 (20-08-2018)

Identifiers

Cite

Laurent Marichal, Jean-Philippe Renault, Stéphane Chédin, Gilles Lagniel, Géraldine Klein, et al.. Importance of Post-translational Modifications in the Interaction of Proteins with Mineral Surfaces: The Case of Arginine Methylation and Silica surfaces. Langmuir, 2018, 34 (18), pp.5312 - 5322. ⟨10.1021/acs.langmuir.8b00752⟩. ⟨cea-01858455⟩
87 View
0 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More