Article Sidebar
Published:
May 4, 2017Keywords:
Article Details
Submission of a manuscript to this journal is a representation that the manuscript has not been published previously and is not under consideration for publication elsewhere.
All authors named in each manuscript would be required to sign a form (to be supplied by the Editor) so that they may retain their copyright in the article but to assign to us (the Publishers) and its licensees in perpetuity, in all forms, formats and media (whether known or created in the future) to (i) publish, reproduce, distribute, display and store the contribution, (ii) translate the contribution into other languages, create adaptations, reprints, include within collections and create summaries, extracts and/or abstracts of the contribution, (iii) create any other derivative works(s) based on the contribution, (iv) to exploit all subsidiary rights in the contribution, (v) the inclusion of electronic links from the contribution to third party material where-ever it may be located, and (vi) license any thrid party to do any or all of the above.
Main Article Content
Determination of activities of human carbonic anhydrase II inhibitors from curcumin analogs
Abstract
Purpose: To evaluate the activities of new curcumin analogs as carbonic anhydrase II (CA-II) inhibitor.
Methods: Carbonic anhydrase II (CA-II) inhibition was determined by each ligand capability to inhibit the esterase activity of CA-II using 4-NPA as a substrate in 96-well plates. Dimethyl sulfoxide was used to dissolve each curcumin analog compound, and then diluted with biological buffer. They were then mixed with CA-II solution and to start the reaction, 4-NPA was added. Hydrolysis of the substrate was evaluated at 405 nm after incubation for 2 h at 25 °C. The IC50 value of compounds with inhibitory activity higher than 40 % was then evaluated. Molecular docking was also used to predict enzymeinhibitor interaction.
Results: Eight new curcumin analogs were potent to inhibit CA-II activity with IC50 values ranging from 7.92 ± 0.54 to 72.31 ± 2.21 μmol; the lowest value was exhibited by (3E,5E)-3,5-bis[(2- hydroxyphenyl)methylidene]piperidin-4-one (a1). Molecular docking analysis revealed that this molecule formed hydrogen bonds with Thr199, Thr200 and Gln92 at the active site of CA-II.
Conclusion: These curcumin analogs have inhibitory potential against CA-II; (3E, 5E)-3,5-bis[(2- hydroxyphenyl)methylidene]piperidin-4-one (a1) has the highest inhibitory activity and may be useful in the development of CA-II inhibitors for glaucoma treatment.
Keywords: Carbonic anhydrase II inhibitor, Curcumin analogs, Molecular docking
