Title of article :
Urease and α-chymotrypsin inhibitory activities of transition metal complexes of new Schiff base ligand: Kinetic and thermodynamic studies of the synthesized complexes using TG–DTA pyrolysis
Author/Authors :
Muhammad Ikram، نويسنده , , Sadia Rehman، نويسنده , , Muhammad Ali، نويسنده , , Faridoon Shabani، نويسنده , , Carola Schulzke، نويسنده , , Robert J. Baker، نويسنده , , Alexander J. Blake، نويسنده , , Khan Malook، نويسنده , , Henry Wong، نويسنده , , Saeed-Ur-Rehman، نويسنده ,
Issue Information :
دوهفته نامه با شماره پیاپی سال 2013
Pages :
7
From page :
22
To page :
28
Abstract :
The Schiff base 2-[(E)-(quinolin-3-ylimino)methyl]phenol (H-QMP) was crystallized in Pc space group and complexed with Ni(II) and Co(II) in [M(QMP)2] and Cu(II) and Zn(II) in [M(QMP)(CH3COO)]H2O compositions. Elemental analyses, mass spectrometry, IR, UV–vis spectroscopy, conductance study and magnetic susceptibilities were used to characterize the complexes. The thermograms obtained in the range of 30–1000 °C were used for kinetic and thermodynamic calculations. The activation energies and order of pyrolysis were calculated using Horowitz–Metzger method. The calculated activation energies were subsequently used for the calculations of thermodynamic parameters including ΔS*, ΔH* and ΔG*. It was found that the thermal stability and activation energy follow the order Cu(II) > Ni(II) > Co(II) > Zn(II) and image, respectively. All the compounds were also studied for their urease and α-chymotrypsin inhibition, showing medium to moderate activities for both the enzymes except nickel complex. Nickel complex shows IC50 = 9.9 ± 0.124 μM ± SEM, and the activity was rationalized by carrying out molecular modeling studies.
Keywords :
Schiff base ligand , Kinetic and thermodynamic study , Coordination compounds , Molecular modeling study , Thermo gravimetric analysis , Urease and ?-chymotrypsin inhibitory activities
Journal title :
Thermochimica Acta
Serial Year :
2013
Journal title :
Thermochimica Acta
Record number :
1200470
Link To Document :
بازگشت