Interaction of [VIVO(acac)2] with Human Serum Transferrin and Albumin

被引：41

作者：

Correia, Isabel ^{[1
]}

Chorna, Ielyzaveta ^{[1
]}

Cavaco, Isabel ^{[1
,2
]}

Roy, Somnath ^{[1
,3
]}

Kuznetsov, Maxim L. ^{[1
]}

Ribeiro, Nadia ^{[1
]}

Justino, Goncalo ^{[1
]}

Marques, Fernanda ^{[1
]}

Santos-Silva, Teresa ^{[4
]}

Santos, Marino F. A. ^{[4
]}

Hugo, M. Santos E. ^{[4
,5
]}

Capelo, Jose L. ^{[4
,5
]}

Doutch, James ^{[6
]}

Pessoa, Joao Costa ^{[1
]}

机构：

[1] Univ Lisbon, Ctr Quim Estrutural, Inst Super Tecn, Ave Rovisco Pais, P-1049001 Lisbon, Portugal

[2] Univ Algarve, Dept Quim & Farm, Campus Gambelas, P-8005139 Faro, Portugal

[3] Ananda Chandra Coll, Dept Chem, Jalpaiguri, W Bengal, India

[4] Univ Nova Lisboa, Dept Quim, Fac Ciencias & Tecnol, UCIBIO,REQUIMTE, P-2829516 Caparica, Portugal

[5] PROTEOMASS Sci Soc, Madan Pk,Rua Inventores, P-2825152 Caparica, Portugal

[6] Sci & Technol Facil Council, ISIS Pulsed Neutron & Muon Source, Harwell Sci & Innovat Campus, Didcot OX11 0QX, Oxon, England

来源：

CHEMISTRY-AN ASIAN JOURNAL | 2017年 / 12卷 / 16期

关键词：

acetylacetonate; circular dichroism; mass spectrometry; transferrin; HETEROLEPTIC OXIDOVANADIUM(IV) COMPOUNDS; ANTIDIABETIC VANADIUM COMPLEXES; NUCLEAR DOUBLE-RESONANCE; RAY SOLUTION SCATTERING; RED-BLOOD-CELLS; CRYSTAL-STRUCTURE; OXOVANADIUM(IV) COMPLEXES; N-LOBE; TYROSINE PHOSPHORYLATION; COORDINATION CHEMISTRY;

D O I：

10.1002/asia.201700469

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

VO(acac)(2)] is a remarkable vanadium compound and has potential as a therapeutic drug. It is important to clarify how it is transported in blood, but the reports addressing its binding to serum proteins have been contradictory. We use several spectroscopic and mass spectrometric techniques (ESI and MALDI-TOF), small-angle X-ray scattering and size exclusion chromatography (SEC) to characterize solutions containing [VO(acac)(2)] and either human serum apotransferrin (apoHTF) or albumin (HSA). DFT and modeling protein calculations are carried out to disclose the type of binding to apoHTF. The measured circular dichroism spectra, SEC and MALDI-TOF data clearly prove that at least two VOacac moieties may bind to apoHTF, most probably forming [(VO)-O-IV(acac)(apoHTF)] complexes with residues of the HTF binding sites. No indication of binding of [VO(acac)(2)] to HSA is obtained. We conclude that (VO)-O-IV-acac species may be transported in blood by transferrin. At very low complex concentrations speciation calculations suggest that [(VO)(apoHTF)] species form.

引用

页码：2062 / 2084

页数：23

共 140 条

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