Monitoring peptide tyrosine nitration by spectroscopic methods
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00540887" target="_blank" >RIV/61388963:_____/21:00540887 - isvavai.cz</a>
Alternative codes found
RIV/60461373:22330/21:43922224
Result on the web
<a href="https://doi.org/10.1007/s00726-020-02911-7" target="_blank" >https://doi.org/10.1007/s00726-020-02911-7</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s00726-020-02911-7" target="_blank" >10.1007/s00726-020-02911-7</a>
Alternative languages
Result language
angličtina
Original language name
Monitoring peptide tyrosine nitration by spectroscopic methods
Original language description
Oxidative stress can lead to various derivatives of the tyrosine residue in peptides and proteins. A typical product is 3-nitro-L-tyrosine residue (Nit), which can affect protein behavior during neurodegenerative processes, such as those associated with Alzheimer's and Parkinson's diseases. Surface enhanced Raman spectroscopy (SERS) is a technique with potential for detecting peptides and their metabolic products at very low concentrations. To explore the applicability to Nit, we use SERS to monitor tyrosine nitration in Met-Enkephalin, rev-Prion protein, and α-synuclein models. Useful nitration indicators were the intensity ratio of two tyrosine marker bands at 825 and 870 cm−1 and a bending vibration of the nitro group. During the SERS measurement, a conversion of nitrotyrosine to azobenzene containing peptides was observed. The interpretation of the spectra has been based on density functional theory (DFT) simulations. The CAM-B3LYP and ωB97XD functionals were found to be most suitable for modeling the measured data. The secondary structure of the α-synuclein models was monitored by electronic and vibrational circular dichroism (ECD and VCD) spectroscopies and modeled by molecular dynamics (MD) simulations. The results suggest that the nitration in these peptides has a limited effect on the secondary structure, but may trigger their aggregation.
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
10403 - Physical chemistry
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
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Amino Acids
ISSN
0939-4451
e-ISSN
1438-2199
Volume of the periodical
53
Issue of the periodical within the volume
4
Country of publishing house
AT - AUSTRIA
Number of pages
16
Pages from-to
517-532
UT code for WoS article
000590203400001
EID of the result in the Scopus database
2-s2.0-85096137955