期刊
JOURNAL OF INORGANIC BIOCHEMISTRY
卷 200, 期 -, 页码 -出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2019.110800
关键词
cis-Dioxidovanadium(V) complexes; Human serum albumin; Tyrosinase activity; Acetylcholinesterase activity
资金
- Brazilian funding agency: Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
- Brazilian funding agency: Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Brazilian funding agency: Fundacao de Amparo a Pesquisa do Estado do Rio Grande do Sul (FAPERGS)
- FAPERGS [17/2551-0000963-0]
- CNPq [424515/2018-4, 303011/2016-5, 409150/2018-5, 304711/2018-7]
The present study reports the biological evaluation of vanadium(V) complexes (1-3) against three different proteins: tyrosinase, acetylcholinesterase (AChE), and human serum albumin (HSA), which were studied by spectroscopic techniques and molecular docking. Despite the synthesis and characterization of complexes 1 and 2 having already previously described, complex 3 is a novel dioxidovanadium(V) derivative. Complex 1 can activate both tyrosinase and AChE enzymes in about 11.5 and 47.0%, respectively. On the other hand, complexes 2 and 3 inhibited the same enzymes (1.30 and 46.0% for tyrosinase and 20.0 and 21.9% for AChE, respectively). Molecular docking calculations suggested that the presence of the hydroxyl group in complex 1 is essential to activate tyrosinase enzymes. According to theoretical analysis, hydrogen bonding, van der Waals, and hydrophobic forces are the main binding interactions for each V(V) complex and AChE. Moreover, the interaction between HSA and vanadium(V) complexes occurs via ground-state association, being only enthalpically driven for complexes 1 and 2 and entropically and enthalpically driven for complex 3. The interaction is spontaneous for all samples and the binding modes do not perturb significantly the secondary and surface structures of the albumin. As there are few reported cases in the literature that explore vanadium complexes against these three proteins, the present results may contribute to future studies by offering different scaffolds to design new vanadium(V) complexes in the hyperpigmentation process and Alzheimer's disease.
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