Syntheses, structures, and bioactivities evaluation of three transition metal complexes with 1,2,4-triazole carboxylic derivative

Yu, Zhongbo; Li, Yong-Hang; Jiang, Shi‐Bin; Wang, Shi-Ling; Qian, Shao‐Song; Qin, Jie; Ma, Jian‐Ping; Li, Juan

doi:10.1080/00958972.2021.1900832

Cited by 1 publication

(1 citation statement)

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“…Additionally, Zn(II) is abundantly found trace element in biological system together with iron and are vital component of most of the metallo-proteins [29][30][31][32]. Particularly, Zn(II) complexes bearing nitrogen containing ligands, with various functionalities, are considered to be privileged systems owing to their versatility and promising urease inhibitory potential [33][34][35][36][37][38][39][40][41]. Keeping in view the versatility of amine based ligands and biocompatible importance of zinc complexes, we herein reported the synthesis, characterization Zn(II) complexes bearing thiophenyl and furyl based chiral amines and their in vitro urease inhibitory effects.…”

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confidence: 99%

Synthesis, characterization and urease inhibitory activities of Zn(II) complexes bearing C1-symmetric ligands derived from (R)-phenylethanamine

Nayab¹,

Alam²,

Khan³

et al. 2021

Bull. Chem. Soc. Eth.

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ABSTRACT. A series of Zn(II) complexes, supported with N-substituted phenylethanamine derivatives, [LnZnCl2] (where Ln = LA ((R)-1-phenyl-N-(thiophene-2-ylmethyl)ethanamine; LB (R)-N-(5-meyhylthiophene-2-yl)methyl-1-phenylethanamine; LC ((R)-N-(furan-2-ylmeththyl)-1-phenylethanamine and LD (R)-N-((5-methylfuran-2-yl)methyl)-1-phenylethanamine) were synthesized and characterized. The urease inhibitory activities of these complexes were determined against selected urease inhibitors where [LBZnCl2] was found to be the most prominent inhibitor of Jack bean urease (J. B. urease) (IC50 = 10.39±0.78 μM), whereas the activity of Bacillus pasteurii urease (B. P. urease) was predominantly inhibited by [LAZnCl2] (IC50 = 8.68±0.7 μM). Additionally, MOE-Dock program was used to affirm the probable binding modes of these complexes into the crystal structure of J. B. urease which certainly verified the inhibitory mechanism of these novel complexes. KEY WORDS: Zn(II) complexes, (R)-Phenylethanamine, Urease inhibition, Molecular docking Bull. Chem. Soc. Ethiop. 2021, 35(2), 301-314. DOI: https://dx.doi.org/10.4314/bcse.v35i2.7

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