PEPPSI complexes as potential prodrugs: enzyme inhibition, antioxidant activity, electrochemical characterization, molecular docking analysis
Citation
Üstün, E., Çelebi, M. S., Ayvaz, M. Ç., & Şahin, N. (2021). PEPPSI complexes as potential prodrugs: enzyme inhibition, antioxidant activity, electrochemical characterization, molecular docking analysis. Zeitschrift für Naturforschung C, 76(5-6), 219-227.Abstract
In this study, enzyme inhibition and antioxidant
activity analyzes of previously characterized
pyridine-enhanced precatalyst preparation stabilization
and initiation (PEPPSI)-type Palladium(II) complexes
with benzimidazole-type ligands {dichloro[L]pyridine
palladium(II), L1: 1-(2-methyl-2-propenyl)-3-[benzylbenzimidazole]-
2-ylidene, L2: 1-(2-methyl-2-propenyl)-3-[4-
chloro benzylbenzimidazole]-2-ylidene, L3: 1-(2-methyl-
2-propenyl)-3-[3-methylbenzylbenzimidazole]-2-ylidene,
L4: 1-(2-methyl-2-propenyl)-3-[3,4,5-thrimethoxybenzylb
-enzimidazole]-2-ylidene, L5: 1-(2-methyl-2-propenyl)-3-
[3-naphthylbenzylbenzimidazole]-2-ylidene, L6: 1-(2-met
-hyl-2-propenyl)-3-[anthracen-9-ylmethylbenzimidazole]
-2-ylidene}were performed and evaluated as potential drugs
for neurodegenerative disorders such as Alzheimer disease
and Parkinson disease. Inhibition of tyrosinase enzyme of
N-heterocyclic carbenes (NHC) complexes was determined
for the first time in literature. Chelating activities of the
complexes were determined and compared with EDTA.
Electrochemical characterization was performed using cyclic
voltammetry method. Moreover, global reactivity descriptors
and electronic transitions were evaluated by DFT/
TDDFT methods and molecular docking interactions with
human acetylcholine esterase, human butyrylcholine
esterase and oxidoreductase were studied.
Source
Zeitschrift für Naturforschung C,Volume
76Issue
5-6URI
https://www.degruyter.com/document/doi/10.1515/znc-2020-0295/htmlhttps://hdl.handle.net/20.500.12418/12986