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Sticky salts: overbinding of monovalent cations to phosphorylations in all-atom forcefields

Jules MarieniD, Julie Puyo-FourtineiD, Chantal PrévostiD, Sophie Sacquin‐MoraiD, Élise Duboué-DijoniD

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Abstract

Phosphorylation is a major post-translational modification, which is involved in the regulation of the dynamics and function of Intrinsically Disordered Proteins (IDPs). We recently characterized a phenomenon, which we termed n-Phosphate collaborations (nP-collabs), where bulk cations form stable bridges between several phosphoresidues in all-atom molecular dynamic simulations. nP-collabs were found to be sensitive to the combination of forcefields and cation types. Here, we attempt to assess the physical relevance of these nP-collabs by evaluating the strength of the cation/phosphate interaction through osmotic coefficient ({phi}) calculations on the model [Formula] and [Formula] salts, using different classical forcefields for phosphorylations. All force-fields were found to overestimate the strength of the interaction to various degrees. We thus designed new parameters for CHARMM36m and AmberFF99SB-ILDN using the Electronic Continuum Correction (ECC) approach, which provide remarkable agreement for{phi} values for both cation types and over a range of concentrations. We provide a preliminary test of these ECC parameters for phosphorylations by simulating the sevenfold-phosphorylated rhodopsin peptide 7PP and comparing secondary chemical shifts to experimental data. Conformational ensembles resulting from the ECC-derived phosphorylated forcefields display both qualitative and quantitative improvements with regard to full-charge forcefields. We thus conclude that long-lasting nP-collabs are artifacts for classical forcefields born from the lack of explicit polarization, and propose a possible computational strategy for the extensive parameterization of phosphorylations. The presence of long-lived nP-collabs in simulations produced using classical forcefields is therefore a serious concern for the accurate modelling of multiphosphorylated peptides and IDPs, which are at the center of research questions regarding neurodegenerative diseases such as Alzheimers or Parkinsons.

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