Photochemical Synthesis of Pink Silver and Its Use for Monitoring Peptide Nitration Via Surface Enhanced Raman Spectroscopy (SERS)

Overview

Journal Amino Acids

Specialty Biochemistry

Date 2022 Jun 22

PMID 35731286

Authors

Marina Sokolova

Hana Sestakova

Martin Truksa

Martin Safarik

Romana Hadravova

Petr Bour

Jaroslav Sebestik

Affiliations

Soon will be listed here.

Abstract

Oxidative stress may cause extended tyrosine posttranslational modifications of peptides and proteins. The 3-nitro-L-tyrosine (Nit), which is typically formed, affects protein behavior during neurodegenerative processes, such as Alzheimer's and Parkinson's diseases. Such metabolic products may be conveniently detected at very low concentrations by surface enhanced Raman spectroscopy (SERS). Previously, we have explored the SERS detection of the Nit NO bending vibrational bands in a presence of hydrogen chloride (Niederhafner et al., Amino Acids 53:517-532, 2021, ibid). In this article, we describe performance of a new SERS substrate, "pink silver", synthesized photochemically. It provides SERS even without the HCl induction, and the acid further decreases the detection limit about 9 times. Strong SERS bands were observed in the asymmetric (1550-1475 cm) and symmetric (1360-1290 cm) NO stretching in the NO group. The bending vibration was relatively weak, but appeared stronger when HCl was added. The band assignments were supported by density functional theory modeling.

Citing Articles

Discrimination and Quantification of Glutathione by Cu-Based Nanozymes.

Liu M, Yan C, Ye Q, Sun X, Han J Biosensors (Basel). 2023; 13(8).

PMID: 37622913 PMC: 10452140. DOI: 10.3390/bios13080827.

References

Abello N, Kerstjens H, Postma D, Bischoff R . Protein tyrosine nitration: selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins. J Proteome Res. 2009; 8(7):3222-38. DOI: 10.1021/pr900039c. View

Abello N, Barroso B, Kerstjens H, Postma D, Bischoff R . Chemical labeling and enrichment of nitrotyrosine-containing peptides. Talanta. 2010; 80(4):1503-12. DOI: 10.1016/j.talanta.2009.02.002. View

Aslan M, Dogan S . Proteomic detection of nitroproteins as potential biomarkers for cardiovascular disease. J Proteomics. 2011; 74(11):2274-88. DOI: 10.1016/j.jprot.2011.05.029. View

Beal M, Ferrante R, Browne S, Matthews R, Kowall N, Brown Jr R . Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann Neurol. 1997; 42(4):644-54. DOI: 10.1002/ana.410420416. View

Beckman J, Crow J . Pathological implications of nitric oxide, superoxide and peroxynitrite formation. Biochem Soc Trans. 1993; 21(2):330-4. DOI: 10.1042/bst0210330. View

Beckman J, Beckman T, Chen J, Marshall P, Freeman B . Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci U S A. 1990; 87(4):1620-4. PMC: 53527. DOI: 10.1073/pnas.87.4.1620. View

Beeckmans S, Kanarek L . The modification with tetranitromethane of an essential tyrosine in the active site of pig fumarase. Biochim Biophys Acta. 1983; 743(3):370-8. DOI: 10.1016/0167-4838(83)90395-3. View

Betz J, Yu W, Cheng Y, White I, Rubloff G . Simple SERS substrates: powerful, portable, and full of potential. Phys Chem Chem Phys. 2013; 16(6):2224-39. DOI: 10.1039/c3cp53560f. View

Burai R, Ait-Bouziad N, Chiki A, Lashuel H . Elucidating the Role of Site-Specific Nitration of α-Synuclein in the Pathogenesis of Parkinson's Disease via Protein Semisynthesis and Mutagenesis. J Am Chem Soc. 2015; 137(15):5041-52. DOI: 10.1021/ja5131726. View

10.

Campolo N, Issoglio F, Estrin D, Bartesaghi S, Radi R . 3-Nitrotyrosine and related derivatives in proteins: precursors, radical intermediates and impact in function. Essays Biochem. 2020; 64(1):111-133. DOI: 10.1042/EBC20190052. View

11.

Castro L, Demicheli V, Tortora V, Radi R . Mitochondrial protein tyrosine nitration. Free Radic Res. 2010; 45(1):37-52. DOI: 10.3109/10715762.2010.516254. View

12.

Chang C, Chen Y, Huang Y, Lai C, Jeng U, Lai Y . Nanostructured silver dendrites for photon-induced Cysteine dimerization. Sci Rep. 2019; 9(1):20174. PMC: 6934660. DOI: 10.1038/s41598-019-56517-5. View

13.

Das M, Gangopadhyay D, Sebestik J, Habartova L, Michal P, Kapitan J . Chiral detection by induced surface-enhanced Raman optical activity. Chem Commun (Camb). 2021; 57(52):6388-6391. DOI: 10.1039/d1cc01504d. View

14.

De Filippis V, Frasson R, Fontana A . 3-Nitrotyrosine as a spectroscopic probe for investigating protein protein interactions. Protein Sci. 2006; 15(5):976-86. PMC: 2242503. DOI: 10.1110/ps.051957006. View

15.

Duda J, Giasson B, Chen Q, Gur T, Hurtig H, Stern M . Widespread nitration of pathological inclusions in neurodegenerative synucleinopathies. Am J Pathol. 2000; 157(5):1439-45. PMC: 1885725. DOI: 10.1016/S0002-9440(10)64781-5. View

16.

Ferrer-Sueta G, Campolo N, Trujillo M, Bartesaghi S, Carballal S, Romero N . Biochemistry of Peroxynitrite and Protein Tyrosine Nitration. Chem Rev. 2018; 118(3):1338-1408. DOI: 10.1021/acs.chemrev.7b00568. View

17.

Furth A, Hope D . Studies on the chemical modification of the tyrosine residue in bovine neurophysin-II. Biochem J. 1970; 116(4):545-53. PMC: 1185398. DOI: 10.1042/bj1160545. View

18.

Giasson B, Duda J, Murray I, Chen Q, Souza J, Hurtig H . Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions. Science. 2000; 290(5493):985-9. DOI: 10.1126/science.290.5493.985. View

19.

Graham D, Thompson D, Smith W, Faulds K . Control of enhanced Raman scattering using a DNA-based assembly process of dye-coded nanoparticles. Nat Nanotechnol. 2008; 3(9):548-51. DOI: 10.1038/nnano.2008.189. View

20.

Guerrini L, Graham D . Molecularly-mediated assemblies of plasmonic nanoparticles for Surface-Enhanced Raman Spectroscopy applications. Chem Soc Rev. 2012; 41(21):7085-107. DOI: 10.1039/c2cs35118h. View