4.6 Article

Evaluation of Ionic Liquids and Ionic Liquids Active Pharmaceutical Ingredients Inhibition in Elastase Enzyme Activity

期刊

MOLECULES
卷 26, 期 1, 页码 -

出版社

MDPI
DOI: 10.3390/molecules26010200

关键词

ionic liquids; ionic liquids active pharmaceutical ingredients; enzyme activity; elastase; inhibition

资金

  1. European Union (FEDER funds) [POCI/01/0145/FEDER/007265]
  2. FCT/MEC, Fundacao para a Ciencia e Tecnologia [PT2020 UID/QUI/50006/2013]
  3. FCT/MEC, Ministerio da Educacao e Ciencia [PT2020 UID/QUI/50006/2013]
  4. FEDER-Fundo Europeu de Desenvolvimento Regional funds through the COMPETE 2020-Operational Programme for Competitiveness and Internationalization (POCI), Portugal 2020 [POCI-01-0145-FEDER-030163]
  5. FCT [SFRH/BD/138835/2018]
  6. Fundação para a Ciência e a Tecnologia [SFRH/BD/138835/2018] Funding Source: FCT

向作者/读者索取更多资源

This study demonstrated the varying inhibitory effects of ionic liquids and ionic liquids active pharmaceutical ingredients on elastase enzyme activity, with tetrabutylammonium acetate being the most toxic and 1-butyl-3-methylimidazolium acetate being the least toxic.
Human neutrophil elastase (HNE) is used as diagnostic biomarker for inflammation/infection. In this work, 10 ionic liquids (ILs) and 11 ionic liquids active pharmaceutical ingredients (ILs-APIs) were tested to evaluate the inhibition effect on the activity of porcine pancreatic elastase enzyme, frequently employed as a model for HNE. The insertion of ionic liquids in some drugs is useful, as the insertion of ILs with inhibitory capacity will also slow down all processes in which this enzyme is involved. Therefore, a spectrophotometric method was performed to the determination of EC50 values of the compounds tested. EC50 values of 124 +/- 4 mM to 289 +/- 11 mM were obtained, with the most toxic IL for elastase being tetrabutylammonium acetate and the least toxic 1-butyl-3-methylimidazolium acetate. Moreover, sodium salicylate (raw material) presented the lower and benzethonium bistriflimide the higher EC50 when compared with all the IL-APIs tested. This work provides significant information about the effect of the studied IL and IL-APIs in elastase enzyme activity.

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