Publication Type |
Journal Article |
Title |
Binding of (VO2+)-O-IV, (VOL)-O-IV, (VOL2)-O-IV and (VO2L)-O-V Moieties to Proteins: X-ray/Theoretical Characterization and Biological Implications |
Authors |
Marino F. A. Santos Giuseppe Sciortino Isabel Correia Andreia C. P. Fernandes Teresa Santos-Silva Federico Pisanu Eugenio Garribba J.C. Pessoa |
Groups |
BIOIN |
Journal |
CHEMISTRY-A EUROPEAN JOURNAL |
Year |
2022 |
Month |
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|
Volume |
28 |
Number |
40 |
Pages |
|
Abstract |
Vanadium compounds have frequently been proposed as therapeutics, but their application has been hampered by the lack of information on the different V-containing species that may form and how these interact with blood and cell proteins, and with enzymes. Herein, we report several resolved crystal structures of lysozyme with bound (VO2+)-O-IV and (VOL2+)-O-IV, where L=2,2 -bipyridine or 1,10-phenanthroline (phen), and of trypsin with (VO)-O-IV(picolinato)(2) and (VO2)-O-V(phen)(+) moieties. Computational studies complete the refinement and shed light on the relevant role of hydrophobic interactions, hydrogen bonds, and microsolvation in stabilizating the structure. Noteworthy is that the trypsin-(VO2)-O-V(phen) and trypsin-(VO)-O-IV(OH)(phen) adducts correspond to similar energies, thus suggesting a possible interconversion under physiological/biological conditions. The obtained data support the relevance of hydrolysis of V-IV and V-V complexes in the several types of binding established with proteins and the formation of different adducts that might contribute to their pharmacological action, and significantly widen our knowledge of vanadium-protein interactions. |
DOI |
http://dx.doi.org/10.1002/chem.202200105 |
ISBN |
|
Publisher |
WILEY-V C H VERLAG GMBH |
Book Title |
|
ISSN |
0947-6539 |
EISSN |
1521-3765 |
Conference Name |
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Bibtex ID |
WOS:000807742300001 |
Observations |
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