TUTCRIS - Tampereen teknillinen yliopisto

TUTCRIS

Accurate Binding of Sodium and Calcium to a POPC Bilayer by Effective Inclusion of Electronic Polarization

Tutkimustuotosvertaisarvioitu

Standard

Accurate Binding of Sodium and Calcium to a POPC Bilayer by Effective Inclusion of Electronic Polarization. / Melcr, Josef; Martinez-Seara, Hector; Nencini, Ricky; Kolafa, Jiří; Jungwirth, Pavel; Ollila, O. H. Samuli.

julkaisussa: Journal of Physical Chemistry B, Vuosikerta 122, Nro 16, 26.04.2018, s. 4546-4557.

Tutkimustuotosvertaisarvioitu

Harvard

Melcr, J, Martinez-Seara, H, Nencini, R, Kolafa, J, Jungwirth, P & Ollila, OHS 2018, 'Accurate Binding of Sodium and Calcium to a POPC Bilayer by Effective Inclusion of Electronic Polarization', Journal of Physical Chemistry B, Vuosikerta. 122, Nro 16, Sivut 4546-4557. https://doi.org/10.1021/acs.jpcb.7b12510

APA

Melcr, J., Martinez-Seara, H., Nencini, R., Kolafa, J., Jungwirth, P., & Ollila, O. H. S. (2018). Accurate Binding of Sodium and Calcium to a POPC Bilayer by Effective Inclusion of Electronic Polarization. Journal of Physical Chemistry B, 122(16), 4546-4557. https://doi.org/10.1021/acs.jpcb.7b12510

Vancouver

Melcr J, Martinez-Seara H, Nencini R, Kolafa J, Jungwirth P, Ollila OHS. Accurate Binding of Sodium and Calcium to a POPC Bilayer by Effective Inclusion of Electronic Polarization. Journal of Physical Chemistry B. 2018 huhti 26;122(16):4546-4557. https://doi.org/10.1021/acs.jpcb.7b12510

Author

Melcr, Josef ; Martinez-Seara, Hector ; Nencini, Ricky ; Kolafa, Jiří ; Jungwirth, Pavel ; Ollila, O. H. Samuli. / Accurate Binding of Sodium and Calcium to a POPC Bilayer by Effective Inclusion of Electronic Polarization. Julkaisussa: Journal of Physical Chemistry B. 2018 ; Vuosikerta 122, Nro 16. Sivut 4546-4557.

Bibtex - Lataa

@article{db660d2d3d394d0bba940cee5f37cc35,
title = "Accurate Binding of Sodium and Calcium to a POPC Bilayer by Effective Inclusion of Electronic Polarization",
abstract = "Binding affinities and stoichiometries of Na+ and Ca2+ ions to phospholipid bilayers are of paramount significance in the properties and functionality of cellular membranes. Current estimates of binding affinities and stoichiometries of cations are, however, inconsistent due to limitations in the available experimental and computational methods. In this work, we improve the description of the binding details of Na+ and Ca2+ ions to a 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) bilayer by implicitly including electronic polarization as a mean field correction, known as the electronic continuum correction (ECC). This is applied by scaling the partial charges of a selected state-of-the-art POPC lipid model for molecular dynamics simulations. Our improved ECC-POPC model reproduces not only the experimentally measured structural parameters for the ion-free membrane, but also the response of lipid headgroup to a strongly bound cationic amphiphile, as well as the binding affinities of Na+ and Ca2+ ions. With our new model, we observe on the one side negligible binding of Na+ ions to POPC bilayer, while on the other side stronger interactions of Ca2+ primarily with phosphate oxygens, which is in agreement with the previous interpretations of the experimental spectroscopic data. The present model results in Ca2+ ions forming complexes with one to three POPC molecules with almost equal probabilities, suggesting more complex binding stoichiometries than those from simple models used to interpret the NMR data previously. The results of this work pave the way to quantitative molecular simulations with realistic electrostatic interactions of complex biochemical systems at cellular membranes.",
author = "Josef Melcr and Hector Martinez-Seara and Ricky Nencini and Jiř{\'i} Kolafa and Pavel Jungwirth and Ollila, {O. H. Samuli}",
note = "EXT=”Martinez-Seara, Hector” EXT={"}Ollila, O. H. Samuli{"}",
year = "2018",
month = "4",
day = "26",
doi = "10.1021/acs.jpcb.7b12510",
language = "English",
volume = "122",
pages = "4546--4557",
journal = "Journal of Physical Chemistry Part B",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "16",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - Accurate Binding of Sodium and Calcium to a POPC Bilayer by Effective Inclusion of Electronic Polarization

AU - Melcr, Josef

AU - Martinez-Seara, Hector

AU - Nencini, Ricky

AU - Kolafa, Jiří

AU - Jungwirth, Pavel

AU - Ollila, O. H. Samuli

N1 - EXT=”Martinez-Seara, Hector” EXT="Ollila, O. H. Samuli"

PY - 2018/4/26

Y1 - 2018/4/26

N2 - Binding affinities and stoichiometries of Na+ and Ca2+ ions to phospholipid bilayers are of paramount significance in the properties and functionality of cellular membranes. Current estimates of binding affinities and stoichiometries of cations are, however, inconsistent due to limitations in the available experimental and computational methods. In this work, we improve the description of the binding details of Na+ and Ca2+ ions to a 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) bilayer by implicitly including electronic polarization as a mean field correction, known as the electronic continuum correction (ECC). This is applied by scaling the partial charges of a selected state-of-the-art POPC lipid model for molecular dynamics simulations. Our improved ECC-POPC model reproduces not only the experimentally measured structural parameters for the ion-free membrane, but also the response of lipid headgroup to a strongly bound cationic amphiphile, as well as the binding affinities of Na+ and Ca2+ ions. With our new model, we observe on the one side negligible binding of Na+ ions to POPC bilayer, while on the other side stronger interactions of Ca2+ primarily with phosphate oxygens, which is in agreement with the previous interpretations of the experimental spectroscopic data. The present model results in Ca2+ ions forming complexes with one to three POPC molecules with almost equal probabilities, suggesting more complex binding stoichiometries than those from simple models used to interpret the NMR data previously. The results of this work pave the way to quantitative molecular simulations with realistic electrostatic interactions of complex biochemical systems at cellular membranes.

AB - Binding affinities and stoichiometries of Na+ and Ca2+ ions to phospholipid bilayers are of paramount significance in the properties and functionality of cellular membranes. Current estimates of binding affinities and stoichiometries of cations are, however, inconsistent due to limitations in the available experimental and computational methods. In this work, we improve the description of the binding details of Na+ and Ca2+ ions to a 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) bilayer by implicitly including electronic polarization as a mean field correction, known as the electronic continuum correction (ECC). This is applied by scaling the partial charges of a selected state-of-the-art POPC lipid model for molecular dynamics simulations. Our improved ECC-POPC model reproduces not only the experimentally measured structural parameters for the ion-free membrane, but also the response of lipid headgroup to a strongly bound cationic amphiphile, as well as the binding affinities of Na+ and Ca2+ ions. With our new model, we observe on the one side negligible binding of Na+ ions to POPC bilayer, while on the other side stronger interactions of Ca2+ primarily with phosphate oxygens, which is in agreement with the previous interpretations of the experimental spectroscopic data. The present model results in Ca2+ ions forming complexes with one to three POPC molecules with almost equal probabilities, suggesting more complex binding stoichiometries than those from simple models used to interpret the NMR data previously. The results of this work pave the way to quantitative molecular simulations with realistic electrostatic interactions of complex biochemical systems at cellular membranes.

U2 - 10.1021/acs.jpcb.7b12510

DO - 10.1021/acs.jpcb.7b12510

M3 - Article

VL - 122

SP - 4546

EP - 4557

JO - Journal of Physical Chemistry Part B

JF - Journal of Physical Chemistry Part B

SN - 1520-6106

IS - 16

ER -