دورية أكاديمية
Ammonia Toxicity and Associated Protein Oxidation: A Single-Cell Surface Enhanced Raman Spectroscopy Study
| العنوان: | Ammonia Toxicity and Associated Protein Oxidation: A Single-Cell Surface Enhanced Raman Spectroscopy Study |
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| المؤلفون: | Davide Redolfi-Bristol, Alessandro Mangiameli, Kenta Yamamoto, Elia Marin, Wenliang Zhu, Osam Mazda, Pietro Riello, Giuseppe Pezzotti |
| سنة النشر: | 1753 |
| مصطلحات موضوعية: | Biophysics, Biochemistry, Microbiology, Cell Biology, Genetics, Molecular Biology, Cancer, Hematology, Infectious Diseases, Virology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, size 50 nm, severe skin damage, provide new insights, fluorescence microscopy revealed, enhanced cancer metabolism, containing amino acids, raman signal enhancement, enhanced raman spectroscopy, human dermal fibroblast, cells using surface, 3 , associated protein oxidation, hdf cells showed, protein oxidation, raman vibrations, human body, protein degradation |
| الوصف: | Ammonia (NH 3 ) is a commonly used industrial chemical to which exposure at high concentrations can result in severe skin damage. Moreover, high levels of ammonia in the human body can lead to hyperammonemia conditions and enhanced cancer metabolism. In this work, the toxicity mechanism of NH 3 has been studied against human dermal fibroblast (HDF) cells using surface-enhanced Raman spectroscopy (SERS). For this purpose, gold nanoparticles of size 50 nm have been prepared and used as probes for Raman signal enhancement, after being internalized inside HDF cells. Following the exposure to ammonia, HDF cells showed a significant variation in the protein ternary structure’s signals, demonstrating their denaturation and oxidation process, together with early signs of apoptosis. Meaningful changes were observed especially in the Raman vibrations of sulfur-containing amino acids (cysteine and methionine) together with aromatic residues. Fluorescence microscopy revealed the formation of reactive oxygen and nitrogen species in cells, which confirmed their stressed condition and to whom the causes of protein degradation can be attributed. These findings can provide new insights into the mechanism of ammonia toxicity and protein oxidation at a single-cell level, demonstrating the high potential of the SERS technique in investigating the cellular response to toxic compounds. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | unknown |
| العلاقة: | https://figshare.com/articles/journal_contribution/Ammonia_Toxicity_and_Associated_Protein_Oxidation_A_Single-Cell_Surface_Enhanced_Raman_Spectroscopy_Study/24903463Test |
| DOI: | 10.1021/acs.chemrestox.3c00368.s001 |
| الإتاحة: | https://doi.org/10.1021/acs.chemrestox.3c00368.s001Test https://figshare.com/articles/journal_contribution/Ammonia_Toxicity_and_Associated_Protein_Oxidation_A_Single-Cell_Surface_Enhanced_Raman_Spectroscopy_Study/24903463Test |
| حقوق: | CC BY-NC 4.0 |
| رقم الانضمام: | edsbas.816A2532 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1021/acs.chemrestox.3c00368.s001 |
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