scholarly journals Proline does not quench singlet oxygen: Evidence to reconsider its protective role in plants

2013 ◽  
Vol 64 ◽  
pp. 80-83 ◽  
Author(s):  
Santiago Signorelli ◽  
Juan Bautista Arellano ◽  
Thor Bernt Melø ◽  
Omar Borsani ◽  
Jorge Monza
2012 ◽  
Vol 135 (1) ◽  
pp. 272-279 ◽  
Author(s):  
Gabriela N. Bosio ◽  
Thomas Breitenbach ◽  
Julieta Parisi ◽  
Miguel Reigosa ◽  
Frances H. Blaikie ◽  
...  

Biomedicines ◽  
2021 ◽  
Vol 9 (3) ◽  
pp. 271
Author(s):  
Qingjun Kong ◽  
Qingzhi Zeng ◽  
Jia Yu ◽  
Hongxi Xiao ◽  
Jun Lu ◽  
...  

Resveratrol dimers have been extensively reported on due to their antioxidative activity. Previous studies revealed that resveratrol dimer has been shown to selectively quench singlet oxygen (1O2), and could protect DNA from oxidative damage. The mechanism of resveratrol dimers protecting DNA against oxidative damage is still not clear. Therefore, in this project, the reactants and products of resveratrol dimers protecting guanine from oxidative damage were qualitatively monitored and quantitatively analyzed by UHPLC-QTOF-MS2 and UHPLC-QQQ-MS2. Results showed that when guanine and resveratrol dimers were attacked by 1O2, mostly resveratrol dimers were oxidized, which protected guanine from oxidation. Resveratrol dimers’ oxidation products were identified and quantified at m/z 467.1134 [M-H]− and 467.1118 [M-H]−, respectively. The resorcinol of resveratrol dimers reacted with singlet oxygen to produce p-benzoquinone, protecting guanine from 1O2 damage. Therefore, it is hereby reported for the first time that the resorcinol ring is the characteristic structure in stilbenes inhibiting 1O2 induced-DNA damage, which provides a theoretical basis for preventing and treating DNA damage-mediated diseases.


2010 ◽  
Vol 14 (11) ◽  
pp. 962-967 ◽  
Author(s):  
Roman Dĕdic ◽  
Alexander Molnár ◽  
Antonín Svoboda ◽  
Jan Hála

In this contribution, the influence of lipids on excitation energy transfer from lipophilic photosensitizer tetraphenylporphyrin to oxygen was investigated in chloroform solutions of phosphatidylcholine as well as in bulk lipid. The excited states kinetics were examined in a wide range of lipid concentrations (from zero to the saturated concentration) by direct time- and spectral-resolved detection of weak near infrared phosphorescence of the photosensitizer (around 840 nm) and singlet oxygen (about 1278 nm). While photosensitizer triplet kinetics follows single-exponential decay with lifetime of 0.52 μs in pure chloroform, two distinct components with lifetimes of approximately 0.4 and 1 μs appear after phosphatidylcholine addition. Both the lifetimes exhibit shortening tendency with increasing lipid concentration. Relative weights of the two components depend on the lipid concentration. Singlet oxygen kinetics exhibit single-exponential rise with lifetimes roughly corresponding to the shorter components of photosensitizer decays while their decays require two exponentials. The lifetime of the longer component decreases with increasing concentration of lipid from (77.6 ± 1.3) μ s at pure chloroform to (14.3 ± 1.1) μ s at the saturated lipid concentration. The time-constants obtained in bulk lipid sample follow the above-mentioned trends. Tetraphenylporphyrin photoproduct formation under pulsed excitation in chloroform solutions was demonstrated. The quantum yield of singlet oxygen production of the photoproduct is lower than that of the tetraphenylporphyrin. It was shown that lipids prevent the singlet-oxygen mediated formation of TPP photoproduct, probably by efficient quenching of singlet oxygen. This quenching is justified by shortening of the longer component of singlet oxygen luminescence decays with increasing concentration of the lipid. Moreover, the lipids also quench triplet states of the photosensitizer.


Biomolecules ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 268
Author(s):  
Qingjun Kong ◽  
Xueyan Ren ◽  
Jianrui Qi ◽  
Jia Yu ◽  
Jun Lu ◽  
...  

Stilbenes, particularly resveratrol and resveratrol dimers, could effectively quench singlet oxygen (1O2). It was reported that both resorcinol and carbon-carbon double bond quenching 1O2 can participate in the mechanism. However, it is still not clear which structure plays a dominant role in quenching 1O2. To investigate the characteristic structure in the mechanism of quenching 1O2, the resveratrol, pterostilbene and piceatannol quenching 1O2 abilities were compared by UHPLC-QTOF-MS2 and UHPLC-QQQ-MS2. Results showed that catechol, carbon-carbon double bond and resorcinol participated in the quenching of 1O2. Catechol ring plays a leading role in the mechanism, and the contribution of the structures in quenching 1O2 activity are as follows: catechol ring > carbon-carbon double bond > resorcinol ring, which is supported by the calculation of energy. Our findings will contribute to the future screening of stilbenes with higher activity, and those stilbenes may have great therapeutic potential in 1O2-mediated diseases.


2007 ◽  
Vol 282 (35) ◽  
pp. 25577-25587 ◽  
Author(s):  
Tiago Rodrigues ◽  
Lucimar P. de França ◽  
Cintia Kawai ◽  
Priscila A. de Faria ◽  
Katia C. U. Mugnol ◽  
...  

2013 ◽  
Vol 250 (12) ◽  
pp. 2539-2543 ◽  
Author(s):  
Peter Boldog ◽  
Kata Hajdu ◽  
Melinda Magyar ◽  
Éva Hideg ◽  
Klara Hernádi ◽  
...  

2020 ◽  
Vol 134 (1) ◽  
pp. 71-72
Author(s):  
Naseer Ahmed ◽  
Masooma Naseem ◽  
Javeria Farooq

Abstract Recently, we have read with great interest the article published by Ibarrola et al. (Clin. Sci. (Lond.) (2018) 132, 1471–1485), which used proteomics and immunodetection methods to show that Galectin-3 (Gal-3) down-regulated the antioxidant peroxiredoxin-4 (Prx-4) in cardiac fibroblasts. Authors concluded that ‘antioxidant activity of Prx-4 had been identified as a protein down-regulated by Gal-3. Moreover, Gal-3 induced a decrease in total antioxidant capacity which resulted in a consequent increase in peroxide levels and oxidative stress markers in cardiac fibroblasts.’ We would like to point out some results stated in the article that need further investigation and more detailed discussion to clarify certain factors involved in the protective role of Prx-4 in heart failure.


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