Advanced search
1 file | 4.55 MB Add to list

Absolute configuration and biological profile of pyrazoline enantiomers as MAO inhibitory activity

(2019) CHIRALITY. 31(1). p.21-33
Author
Organization
Abstract
A new racemic pyrazoline derivative was synthesized and resolved to its enantiomers using analytic and semipreparative high-pressure liquid chromatography. The absolute configuration of both fractions was established using vibrational circular dichroism. The in vitro monoamine oxidase (MAO) inhibitory profiles were evaluated for the racemate and both enantiomers separately for the two isoforms of the enzyme. The racemic compound and both enantiomers were found to inhibit hMAO-A selectively and competitively. In particular, the R enantiomer was detected as an exceptionally potent and a selective MAO-A inhibitor (K-i = 0.85 x 10(-3) +/- 0.05 x 10(-3) mu M and SI: 2.35 x 10(-5)), whereas S was determined as poorer compound than R in terms of K-i and SI (0.184 +/- 0.007 and 0.001). The selectivity of the enantiomers was explained by molecular modeling docking studies based on the PDB enzymatic models of MAO isoforms.
Keywords
2-pyrazoline, molecular modeling docking, monoamine oxidase inhibitory activity, specific rotation, stereochemistry, vibrational circular dichroism, MONOAMINE-OXIDASE-B, FORCE-FIELD, RAT-BRAIN, DERIVATIVES, POPULATIONS, CHALCONES, DISEASE

Downloads

  • 5-QBHA3-Revisedmanuscript.pdf
    • full text
    • |
    • open access
    • |
    • PDF
    • |
    • 4.55 MB

Citation

Please use this url to cite or link to this publication:

MLA
Goksen, Umut Salgin, et al. “Absolute Configuration and Biological Profile of Pyrazoline Enantiomers as MAO Inhibitory Activity.” CHIRALITY, vol. 31, no. 1, 2019, pp. 21–33.
APA
Goksen, U. S., Sarigul, S., Bultinck, P., Herrebout, W., Dogan, I., Yelekci, K., … Kelekci, N. G. (2019). Absolute configuration and biological profile of pyrazoline enantiomers as MAO inhibitory activity. CHIRALITY, 31(1), 21–33.
Chicago author-date
Goksen, Umut Salgin, Sevgi Sarigul, Patrick Bultinck, Wouter Herrebout, Ilknur Dogan, Kemal Yelekci, Gulberk Ucar, and Nesrin Gokhan Kelekci. 2019. “Absolute Configuration and Biological Profile of Pyrazoline Enantiomers as MAO Inhibitory Activity.” CHIRALITY 31 (1): 21–33.
Chicago author-date (all authors)
Goksen, Umut Salgin, Sevgi Sarigul, Patrick Bultinck, Wouter Herrebout, Ilknur Dogan, Kemal Yelekci, Gulberk Ucar, and Nesrin Gokhan Kelekci. 2019. “Absolute Configuration and Biological Profile of Pyrazoline Enantiomers as MAO Inhibitory Activity.” CHIRALITY 31 (1): 21–33.
Vancouver
1.
Goksen US, Sarigul S, Bultinck P, Herrebout W, Dogan I, Yelekci K, et al. Absolute configuration and biological profile of pyrazoline enantiomers as MAO inhibitory activity. CHIRALITY. 2019;31(1):21–33.
IEEE
[1]
U. S. Goksen et al., “Absolute configuration and biological profile of pyrazoline enantiomers as MAO inhibitory activity,” CHIRALITY, vol. 31, no. 1, pp. 21–33, 2019.
@article{8587731,
  abstract     = {A new racemic pyrazoline derivative was synthesized and resolved to its enantiomers using analytic and semipreparative high-pressure liquid chromatography. The absolute configuration of both fractions was established using vibrational circular dichroism. The in vitro monoamine oxidase (MAO) inhibitory profiles were evaluated for the racemate and both enantiomers separately for the two isoforms of the enzyme. The racemic compound and both enantiomers were found to inhibit hMAO-A selectively and competitively. In particular, the R enantiomer was detected as an exceptionally potent and a selective MAO-A inhibitor (K-i = 0.85 x 10(-3) +/- 0.05 x 10(-3) mu M and SI: 2.35 x 10(-5)), whereas S was determined as poorer compound than R in terms of K-i and SI (0.184 +/- 0.007 and 0.001). The selectivity of the enantiomers was explained by molecular modeling docking studies based on the PDB enzymatic models of MAO isoforms.},
  author       = {Goksen, Umut Salgin and Sarigul, Sevgi and Bultinck, Patrick and Herrebout, Wouter and Dogan, Ilknur and Yelekci, Kemal and Ucar, Gulberk and Kelekci, Nesrin Gokhan},
  issn         = {0899-0042},
  journal      = {CHIRALITY},
  keywords     = {2-pyrazoline,molecular modeling docking,monoamine oxidase inhibitory activity,specific rotation,stereochemistry,vibrational circular dichroism,MONOAMINE-OXIDASE-B,FORCE-FIELD,RAT-BRAIN,DERIVATIVES,POPULATIONS,CHALCONES,DISEASE},
  language     = {eng},
  number       = {1},
  pages        = {21--33},
  title        = {Absolute configuration and biological profile of pyrazoline enantiomers as MAO inhibitory activity},
  url          = {http://dx.doi.org/10.1002/chir.23027},
  volume       = {31},
  year         = {2019},
}

Altmetric
View in Altmetric
Web of Science
Times cited: