Arzu Özel
Karadeniz Technical University
63 Papers
173 Citations
Arzu Özel is an academic researcher from Karadeniz Technical University. The author has contributed to research in topics: Chemistry & Topoisomerase. The author has an hindex of 17, co-authored 59 publications.
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Papers
Tyrosinase inhibition by some flavonoids: Inhibitory activity, mechanism by in vitro and in silico studies.
TL;DR: Flavonoids are main polyphenolic groups widely distributed to fruits, vegetables and beverages the authors consumed daily and found that all the tested materials possessed tyrosinase inhibitory effect compared to the positive control, kojic acid.
102
Discovery of potent α-glucosidase inhibitor flavonols: Insights into mechanism of action through inhibition kinetics and docking simulations.
TL;DR: While sugar substitution to C3-OH of C ring reduced the α-glucosidase inhibitory effect, galloyl substitution to these sugar units increased it, and molecular docking studies were performed to predict their inhibition mechanisms at atomic level.
84
α-Glucosidase inhibitory effect of Potentilla astracanica and some isoflavones: Inhibition kinetics and mechanistic insights through in vitro and in silico studies.
TL;DR: Using molecular modeling techniques, insight is provided into molecular mechanisms of their activity and how allosteric binding of 6 affected binding interactions between the agonist (maltose) and the enzyme.
69
Isolation, production, and characterization of an extracellular lipase from Trichoderma harzianum isolated from soil
TL;DR: It was determined that the best carbon source was glucose and the best nitrogen source was peptone for lipase production and that other metallic ions did not affect the enzyme activity.
Potential of Potentilla inclinata and its polyphenolic compounds in α-glucosidase inhibition: Kinetics and interaction mechanism merged with docking simulations.
TL;DR: In the present study, molecular docking studies were performed to get insights into inhibition mechanisms of the isolates considering their inhibition type using various binding sites of the enzyme model, and revealed that compounds 5 and 7 were competitive, 4 and 6 noncompetitive, and 3 was uncompetitive inhibitors of α-glucosidase enzyme.
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