Coarse-grained model of titrating peptides interacting with lipid bilayers

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Coarse-grained model of titrating peptides interacting with lipid bilayers. / Tesei, Giulio; Vazdar, Mario; Lund, Mikael.

I: The Journal of chemical physics, Vol. 149, Nr. 24, 244108, 2018.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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TY - JOUR

T1 - Coarse-grained model of titrating peptides interacting with lipid bilayers

AU - Tesei, Giulio

AU - Vazdar, Mario

AU - Lund, Mikael

PY - 2018

Y1 - 2018

N2 - Molecular-level computer simulations of peptide aggregation, translocation, and protonation at and in biomembranes are impeded by the large time and length scales involved. We present a computationally efficient, coarse-grained, and solvent-free model for the interaction between lipid bilayers and peptides. The model combines an accurate description of mechanical membrane properties with a new granular representation of the dielectric mismatch between lipids and the aqueous phase. All-atom force fields can be easily mapped onto the coarse-grained model, and parameters for coarse-grained monopeptides accurately extrapolate to membrane permeation free energies for the corresponding dipeptides and tripeptides. Acid-base equilibria of titratable amino acid residues are further studied using a constant-pH ensemble, capturing protonation state changes upon membrane translocation. Important differences between histidine, lysine, and arginine are observed, which are in good agreement with experimental observations.

AB - Molecular-level computer simulations of peptide aggregation, translocation, and protonation at and in biomembranes are impeded by the large time and length scales involved. We present a computationally efficient, coarse-grained, and solvent-free model for the interaction between lipid bilayers and peptides. The model combines an accurate description of mechanical membrane properties with a new granular representation of the dielectric mismatch between lipids and the aqueous phase. All-atom force fields can be easily mapped onto the coarse-grained model, and parameters for coarse-grained monopeptides accurately extrapolate to membrane permeation free energies for the corresponding dipeptides and tripeptides. Acid-base equilibria of titratable amino acid residues are further studied using a constant-pH ensemble, capturing protonation state changes upon membrane translocation. Important differences between histidine, lysine, and arginine are observed, which are in good agreement with experimental observations.

U2 - 10.1063/1.5058234

DO - 10.1063/1.5058234

M3 - Article

VL - 149

JO - Journal of Chemical Physics

T2 - Journal of Chemical Physics

JF - Journal of Chemical Physics

SN - 0021-9606

IS - 24

M1 - 244108

ER -