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Binding of Lanthanide Complexes to Histidine-Containing Peptides Probed 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_____%2F18%3A00491276" target="_blank" >RIV/61388963:_____/18:00491276 - isvavai.cz</a>

  • Alternative codes found

    RIV/60461373:22340/18:43916389

  • Result on the web

    <a href="http://dx.doi.org/10.1002/chem.201800840" target="_blank" >http://dx.doi.org/10.1002/chem.201800840</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/chem.201800840" target="_blank" >10.1002/chem.201800840</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Binding of Lanthanide Complexes to Histidine-Containing Peptides Probed by Raman Optical Activity Spectroscopy

  • Original language description

    Lanthanide complexes are used as convenient spectroscopic probes for many biomolecules. Their binding to proteins is believed to be enhanced by the presence of histidine, but the strength of the interaction significantly varies across different systems. To understand the role of peptide length and sequence, short histidine-containing peptides have been synthesized (His-Gly, His-Gly-Gly, His-Gly-Gly-Gly, Gly-His, Gly-His-Gly, His-His, and Gly-Gly-His) and circularly polarized luminescence (CPL) induced at the [Eu(dpa)(3)](3-) complex has been measured by means of a Raman optical activity (ROA) spectrometer. The obtained data indicate relatively weak binding of the histidine residue to the complex, with a strong participation of other parts of the peptide. Longer peptides, low pH, and a histidine residue close to the N-peptide terminus favor the binding. The binding strengths are approximately proportional to the CPL intensity and roughly correlate with predictions based on molecular dynamics (MD) simulations. The specificity of lanthanide binding to the peptide structure and its intense luminescence and high optical activity make the ROA/CPL technique suitable for probing secondary and tertiary structures of peptides and proteins.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10610 - Biophysics

Result continuities

  • Project

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

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2018

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Chemistry - A European Journal

  • ISSN

    0947-6539

  • e-ISSN

  • Volume of the periodical

    24

  • Issue of the periodical within the volume

    34

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    6

  • Pages from-to

    8664-8669

  • UT code for WoS article

    000435772200026

  • EID of the result in the Scopus database

    2-s2.0-85047484146