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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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
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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