Turkan_2021_J.Biomol.Struct.Dyn_39_3693

Reference

Title : Determination of anticancer properties and inhibitory effects of some metabolic enzymes including acetylcholinesterase, butyrylcholinesterase, alpha glycosidase of some compounds with molecular docking study - Turkan_2021_J.Biomol.Struct.Dyn_39_3693
Author(s) : Turkan F , Taslimi P , Abdalrazaq SM , Aras A , Erden Y , Celebioglu HU , Tuzun B , Agirtas MS , Gulcin I
Ref : J Biomol Struct Dyn , 39 :3693 , 2021
Abstract :

Inhibitory effect of the complexes on some metabolic enzyme results demonstrated that the enzymes inhibited by ligand and it's complex molecules at the micromolar level. The best inhibition effect for alpha-Gly enzyme against cobalt complex with 3.77 +/- 0.58 microM, Ki values were observed. For AChE, and BChE enzymes against SM-Co complex with 74.23 +/- 5.02 microM and 101.21 +/- 12.84 microM Ki values were observed respectively. Molecular docking studies were performed to compare the biological activities of ligands and ligand complexes against enzymes whose names are Achethylcholinesterase (AChE) for ID 4M0E, Butyrylcholinesterase (BChE) for ID 5NN0, alpha glycosidase (alpha-Gly) for ID 1XSI respectively. Anticancer properties of the complexes studied. The doses of all compounds caused significant reductions in MCF-7 cell viability. Zr compound showed the best cytotoxic activity against the MCF-7 cell. SM ligand administered to PC-3 cells exhibited a more pronounced cytotoxic effect than the SM-Co and Zr compounds.

PubMedSearch : Turkan_2021_J.Biomol.Struct.Dyn_39_3693
PubMedID: 32406329

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Citations formats

Turkan F, Taslimi P, Abdalrazaq SM, Aras A, Erden Y, Celebioglu HU, Tuzun B, Agirtas MS, Gulcin I (2021)
Determination of anticancer properties and inhibitory effects of some metabolic enzymes including acetylcholinesterase, butyrylcholinesterase, alpha glycosidase of some compounds with molecular docking study
J Biomol Struct Dyn 39 :3693

Turkan F, Taslimi P, Abdalrazaq SM, Aras A, Erden Y, Celebioglu HU, Tuzun B, Agirtas MS, Gulcin I (2021)
J Biomol Struct Dyn 39 :3693