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The complex nature of calcium cation interactions with phospholipid bilayers

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00466352" target="_blank" >RIV/61388963:_____/16:00466352 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388955:_____/16:00466352

  • Result on the web

    <a href="http://dx.doi.org/10.1038/srep38035" target="_blank" >http://dx.doi.org/10.1038/srep38035</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/srep38035" target="_blank" >10.1038/srep38035</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The complex nature of calcium cation interactions with phospholipid bilayers

  • Original language description

    Understanding interactions of calcium with lipid membranes at the molecular level is of great importance in light of their involvement in calcium signaling, association of proteins with cellular membranes, and membrane fusion. We quantify these interactions in detail by employing a combination of spectroscopic methods with atomistic molecular dynamics simulations. Namely, time-resolved fluorescent spectroscopy of lipid vesicles and vibrational sum frequency spectroscopy of lipid monolayers are used to characterize local binding sites of calcium in zwitterionic and anionic model lipid assemblies, while dynamic light scattering and zeta potential measurements are employed for macroscopic characterization of lipid vesicles in calcium-containing environments. To gain additional atomic-level information, the experiments are complemented by molecular simulations that utilize an accurate force field for calcium ions with scaled charges effectively accounting for electronic polarization effects. We demonstrate that lipid membranes have substantial calcium-binding capacity, with several types of binding sites present. Significantly, the binding mode depends on calcium concentration with important implications for calcium buffering, synaptic plasticity, and protein-membrane association.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CF - Physical chemistry and theoretical chemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2016

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Scientific Reports

  • ISSN

    2045-2322

  • e-ISSN

  • Volume of the periodical

    6

  • Issue of the periodical within the volume

    DEC 2016

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    12

  • Pages from-to

  • UT code for WoS article

    000390018200001

  • EID of the result in the Scopus database

    2-s2.0-85000418318