Coarse-grained model of titrating peptides interacting with lipid bilayers

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 p...

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Bibliographic Details
Published in:The Journal of chemical physics 2018-12, Vol.149 (24), p.244108-244108
Main Authors: Tesei, Giulio, Vazdar, Mario, Lund, Mikael
Format: Article
Language:English
Subjects:
Acid base equilibrium
Chemical Sciences
Computer simulation
Dielectric properties
Fysikalisk kemi
Histidine
Kemi
Lipids
Lysine
Natural Sciences
Naturvetenskap
Peptides
Physical Chemistry
Physics
Protonation
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Summary: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.
ISSN:0021-9606
1089-7690
DOI:10.1063/1.5058234