Journal
CHEMISTRY-AN ASIAN JOURNAL
Volume 12, Issue 16, Pages 2062-2084Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/asia.201700469
Keywords
acetylacetonate; circular dichroism; mass spectrometry; transferrin
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Funding
- Fundacao para a Ciencia e Tecnologia (FCT), Portugal [UID/Multi/04349/2013, UID/QUI/00100/2013, RECI/QEQ-QIN/0189/2012, RECI/QEQMED/0330/2012, PTDC/QEQ-MED/1902/2014, SFRH/BD/77894/2011]
- FCT [IF/00100/2013, IF/00007/2015]
- PROTEOMASS Scientific Society
- UCIBIO, Unidade de Ciencias Biomoleculares Aplicadas [UID/Multi/04378/2013]
- ERDF [POCI-01-0145-FEDER-007728, POCI-01-0145-FEDER-007265]
- Fundação para a Ciência e a Tecnologia [PTDC/QEQ-MED/1902/2014, RECI/QEQ-QIN/0189/2012, SFRH/BD/77894/2011, UID/Multi/04349/2013] Funding Source: FCT
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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.
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