Study on the cytotoxic, antimetastatic and albumin binding properties of the oxidovanadium(IV) chrysin complex. Structural elucidation by computational methodologies.

Autor: Naso LG; CEQUINOR, CONICET/UNLP, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, Bv. 120 Nº 1465, 1900, La Plata, Argentina., Martínez Medina JJ; INIPTA, CONICET/UNCAUS, Universidad Nacional Del Chaco Austral, Comandante Fernández N° 755, Presidencia Roque Sáenz Peña (3700), Chaco, Argentina., Okulik NB; INIPTA, CONICET/UNCAUS, Universidad Nacional Del Chaco Austral, Comandante Fernández N° 755, Presidencia Roque Sáenz Peña (3700), Chaco, Argentina., Ferrer EG; CEQUINOR, CONICET/UNLP, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, Bv. 120 Nº 1465, 1900, La Plata, Argentina., Williams PAM; CEQUINOR, CONICET/UNLP, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, Bv. 120 Nº 1465, 1900, La Plata, Argentina. Electronic address: williams@quimica.unlp.edu.ar.
Jazyk: angličtina
Zdroj: Chemico-biological interactions [Chem Biol Interact] 2022 Jan 05; Vol. 351, pp. 109750. Date of Electronic Publication: 2021 Nov 20.
DOI: 10.1016/j.cbi.2021.109750
Abstrakt: We have previously synthesized and characterized the chrysin coordination complex with the oxidovanadium(IV) cation (V IV O(chrys) 2 ) and characterized in ethanolic solution and in solid state. Because suitable single crystals for X-ray diffraction determinations could not be obtained, in the present work, we elucidate the geometrical parameters of this complex by computational methodologies. The optimization and vibrational investigation were carried out both in ethanolic solution and in gas phase. The computational results support the experimentally proposed geometries of the V IV O(chrys) 2 complex, thus leading to the conclusion that the complex exists as conformers with trans-octahedral geometry in ethanolic solution and as conformers with cis-octahedral geometry in the solid state. The complex also exists as conformers with trans-octahedral geometry in aqueous media. The active species formed after dissolution in DMSO showed anticancer and antimetastatic behavior in human lung cell line A549 with moderate binding (K a ca. 10 5 M -1 ) to bovine serum albumin (BSA). The interaction through hydrogen bonding and van der Waals forces resulted in a spontaneous process. Site marker competitive experiments showed binding sites for chrysin mainly located in site II (subdomain IIIA) and in site I (subdomain IIIA) for the complex. FT-IR spectral measurements showed evidences of the alterations of protein secondary structure in the presence of chrysin and V IV O(chrys) 2 .
(Copyright © 2021 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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