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Chiral sensing of amino acids and proteins chelating with Eu-III complexes by Raman optical activity spectroscopy

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00463863" target="_blank" >RIV/61388963:_____/16:00463863 - isvavai.cz</a>

  • Result on the web

    <a href="http://pubs.rsc.org/en/content/articlehtml/2016/cp/c6cp03968e" target="_blank" >http://pubs.rsc.org/en/content/articlehtml/2016/cp/c6cp03968e</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1039/c6cp03968e" target="_blank" >10.1039/c6cp03968e</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Chiral sensing of amino acids and proteins chelating with Eu-III complexes by Raman optical activity spectroscopy

  • Original language description

    Chiroptical spectroscopy of lanthanides sensitively reflects their environment and finds various applications including probing protein structures. However, the measurement is often hampered by instrumental detection limits. In the present study circularly polarized luminescence (CPL) of a europium complex induced by amino acids is monitored by Raman optical activity (ROA) spectroscopy, which enables us to detect weak CPL bands invisible to conventional CPL spectrometers. In detail, the spectroscopic response to the protonation state could be studied, e.g. histidine at pH = 2 showed an opposite sign of the strongest CPL band in contrast to that at pH = 7. The spectra were interpreted qualitatively on the basis of the ligand-field theory and related to CPL induced by an external magnetic field. Free energy profiles obtained by molecular dynamic simulations for differently charged alanine and histidine forms are in qualitative agreement with the spectroscopic data. The sensitivity and specificity of the detection promise future applications in probing peptide and protein side chains, chemical imaging and medical diagnosis. This potential is observed for human milk and hen egg-white lysozymes; these proteins have a similar structure, but very different induced CPL spectra.

  • 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

    Physical Chemistry Chemical Physics

  • ISSN

    1463-9076

  • e-ISSN

  • Volume of the periodical

    18

  • Issue of the periodical within the volume

    34

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    9

  • Pages from-to

    23803-23811

  • UT code for WoS article

    000382107200042

  • EID of the result in the Scopus database

    2-s2.0-84984823803