dc.contributor.author
Catte, Andrea
dc.contributor.author
Girych, Mykhailo
dc.contributor.author
Javanainen, Matti
dc.contributor.author
Loison, Claire
dc.contributor.author
Melcr, Josef
dc.contributor.author
Miettinen, Markus Sakari
dc.contributor.author
Monticelli, Luca
dc.contributor.author
Määttä, Jukka
dc.contributor.author
Oganesyan, Vasily S.
dc.contributor.author
Ollila, O. H. Samuli
dc.contributor.author
Tynkkynen, Joona
dc.contributor.author
Vilov, Sergey
dc.date.accessioned
2018-06-08T11:02:26Z
dc.date.available
2017-03-23
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/21500
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-24792
dc.description.abstract
Despite the vast amount of experimental and theoretical studies on the binding
affinity of cations – especially the biologically relevant Na+ and Ca2+ – for
phospholipid bilayers, there is no consensus in the literature. Here we show
that by interpreting changes in the choline headgroup order parameters
according to the ‘molecular electrometer’ concept [Seelig et al.,
Biochemistry, 1987, 26, 7535], one can directly compare the ion binding
affinities between simulations and experiments. Our findings strongly support
the view that in contrast to Ca2+ and other multivalent ions, Na+ and other
monovalent ions (except Li+) do not specifically bind to phosphatidylcholine
lipid bilayers at sub-molar concentrations. However, the Na+ binding affinity
was overestimated by several molecular dynamics simulation models, resulting
in artificially positively charged bilayers and exaggerated structural effects
in the lipid headgroups. While qualitatively correct headgroup order parameter
response was observed with Ca2+ binding in all the tested models, no model had
sufficient quantitative accuracy to interpret the Ca2+:lipid stoichiometry or
the induced atomistic resolution structural changes. All scientific
contributions to this open collaboration work were made publicly, using
nmrlipids.blogspot.fi as the main communication platform.
en
dc.format.extent
10 Seiten
dc.rights.uri
http://www.rsc.org/help-legal/legal/copyright-permissions/
dc.subject
ion binding affinity
dc.subject.ddc
500 Naturwissenschaften und Mathematik::530 Physik
dc.subject.ddc
500 Naturwissenschaften und Mathematik::540 Chemie
dc.title
Molecular electrometer and binding of cations to phospholipid bilayers
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
Phys. Chem. Chem. Phys. 18 (2016), 47, S. 32560-32569
dc.identifier.sepid
56298
dcterms.bibliographicCitation.doi
10.1039/C6CP04883H
dcterms.bibliographicCitation.url
http://dx.doi.org/10.1039/C6CP04883H
refubium.affiliation
Physik
de
refubium.affiliation.other
Institut für Theoretische Physik
refubium.funding
OpenAccess Publikation in Allianzlizenz
refubium.mycore.fudocsId
FUDOCS_document_000000026705
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000007952
dcterms.accessRights.openaire
open access
dcterms.isPartOf.issn
1463-9076