UPLC-MS/MS and GC-MS based metabolites profiling of Moringa oleifera seed with its anti- Helicobacter pylori and anti-inflammatory activities.

Compared to its leaf, few studies have been reported on the seeds of Moringa oleifera Lam. Metabolites profiling analysis of M. oleifera seed methanolic extract (ME) and its fixed oil (MO) was attempted via LC/MS and GC/MS. LC/MS analysis of M. oleifera seeds annotated 84 peaks of which glucosinolat...

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Publicado en:Natural Product Research Vol. 36; no. 24; pp. 6433 - 6439
Autores principales: Sayed, Abeer M. El, Omar, Farghaly A., Emam, Marwa Mostafa Abdel-Aziz, Farag, Mohamed A.
Formato: Journal Article
Publicado: Taylor & Francis Ltd Dec2022
Acceso en línea:Ver este registro en EBSCOhost
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      dt: Dec2022
      vid: 36
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      pub: Taylor & Francis Ltd
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        10.1080/14786419.2022.2037088
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        atl: UPLC-MS/MS and GC-MS based metabolites profiling of Moringa oleifera seed with its anti- Helicobacter pylori and anti-inflammatory activities.
      aug:
        au:
          Sayed, Abeer M. El
          Omar, Farghaly A.
          Emam, Marwa Mostafa Abdel-Aziz
          Farag, Mohamed A.
        affil: Pharmacognosy Department, Faculty of Pharmacy, Cairo University, Cairo, Egypt
      sug:
      ab: Compared to its leaf, few studies have been reported on the seeds of Moringa oleifera Lam. Metabolites profiling analysis of M. oleifera seed methanolic extract (ME) and its fixed oil (MO) was attempted via LC/MS and GC/MS. LC/MS analysis of M. oleifera seeds annotated 84 peaks of which glucosinolates and their corresponding acetyl isomers were abundant. GC/MS of seed oil revealed the abundance of fatty acids with oleic acid at 34.3%. ME exhibited significant anti-Helicobacter pylori activity with MIC50 0.92 µg/mL, nearly one-half that of Clarithromycin. Fixed oil (MO) showed a nonselective anti-inflammatory effect with IC50= 24.4 ± 0.8 µg/mL correlated to Ibuprofen. To unravel the mechanism of the anti-H. pylori activity a molecular docking study of the principal components of the ME has been performed, using H. pylori urease enzyme. Interactions with Ni2+ ions and amino acid residue in the active site, which are crucial for the enzyme's biochemical role, are evidenced.
      pubtype: Academic Journal
      doctype: Journal Article
      ougenre: Article
    language: English
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