Monitoring peptide tyrosine nitration by spectroscopic methods

0540887 - ÚOCHB 2022 RIV AT eng J - Článek v odborném periodiku
Niederhafner, Petr - Šafařík, Martin - Neburková, Jitka - Keiderling, T. A. - Bouř, Petr - Šebestík, Jaroslav
Monitoring peptide tyrosine nitration by spectroscopic methods.
Amino Acids. Roč. 53, č. 4 (2021), s. 517-532. ISSN 0939-4451. E-ISSN 1438-2199
Grant CEP: GA ČR(CZ) GA14-00431S; GA ČR(CZ) GA17-00121S; GA ČR(CZ) GA20-10144S; GA MŠMT(CZ) EF16_019/0000729
Institucionální podpora: RVO:61388963
Klíčová slova: nitration * oxidative stress * surface-enhanced Raman spectroscopy (SERS) * vibrational circular dichroism (VCD) * electronic circular dichroism (ECD) * density functional theory (DFT)
Obor OECD: Physical chemistry
Impakt faktor: 3.789, rok: 2021
Způsob publikování: Omezený přístup
https://doi.org/10.1007/s00726-020-02911-7

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.
Trvalý link: http://hdl.handle.net/11104/0318490