Your browser doesn't support javascript.
loading
Effect of central metal ion on some pharmacological properties of new Schiff base complexes. Anticancer, antioxidant, kinetic/thermodynamic and computational studies.
Oveisi Keikha, Alireza; Shahraki, Somaye; Dehghanian, Effat; Mansouri-Torshizi, Hassan.
Afiliación
  • Oveisi Keikha A; Department of Chemistry, University of Sistan and Baluchestan, Zahedan, Iran.
  • Shahraki S; Department of Chemistry, University of Zabol, Zabol, Iran. Electronic address: s-shahraki@uoz.ac.ir.
  • Dehghanian E; Department of Chemistry, University of Sistan and Baluchestan, Zahedan, Iran.
  • Mansouri-Torshizi H; Department of Chemistry, University of Sistan and Baluchestan, Zahedan, Iran.
Spectrochim Acta A Mol Biomol Spectrosc ; 325: 125034, 2024 Aug 25.
Article en En | MEDLINE | ID: mdl-39217954
ABSTRACT
The biological capacities of Schiff Base complexes such as anti-cancer, anti-microbial and anti-oxidant properties have been widely studied in the scientific community. However, the effect of central metal ion in the occurrence of their biological properties should be paid more attention. With this aim, novel 2-(hydroxyimino)-1-phenylpropylidene)benzohydrazide (HIPB) Schiff base ligand, and C1/palladium(II), C2/platinum(II), and C3/zinc(II) complexes derived from it were synthesized and characterized. Theoretical studies showed that C2 is more reactive and also has a higher pharmacological affinity than C1 and C3. Experimental investigations were done to compare some biological properties of the complexes. The anticancer assay showed that C1-C3 have the ability to inhibit the growth of HCT116 colon cancer cell lines, but C2 shows a relatively better effect than other. Antioxidant studies using •DPPH (2,2-diphenyl-1-picrylhydrazyl) assay presented the following trend C2 > C1 > C3 > HIPB. Considering the importance of the antioxidant enzyme catalase in removing reactive oxygen species (ROS), the interaction of C1-C3 with Bovine Liver Catalase (BLC) was evaluated. Kinetic studies showed that C1-C3 can inhibit the catalytic performance of BLC by a similar mechanism, i.e. mixed-type inhibition. Among them, C1 was the strongest inhibitor (Activity inhibition% = 82.2). The C1-C3 quenched the BLC fluorescence emission with dynamic quenching mechanism. The binding affinity to BLC was higher for C1 and C2 than C3. The most important forces in the interaction of C1-C3 with BLC were hydrophobic interactions, which was strongly confirmed by molecular docking data. Tracking the structural changes of catalase showed that BLC undergoes structural changes in the presence of C1 more than C2 and C3.
Palabras clave

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Spectrochim Acta A Mol Biomol Spectrosc Asunto de la revista: BIOLOGIA MOLECULAR Año: 2024 Tipo del documento: Article País de afiliación: Irán Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Spectrochim Acta A Mol Biomol Spectrosc Asunto de la revista: BIOLOGIA MOLECULAR Año: 2024 Tipo del documento: Article País de afiliación: Irán Pais de publicación: Reino Unido