{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,8]],"date-time":"2026-01-08T06:37:34Z","timestamp":1767854254811,"version":"3.49.0"},"reference-count":15,"publisher":"Wiley","issue":"5-6","license":[{"start":{"date-parts":[[2012,7,11]],"date-time":"2012-07-11T00:00:00Z","timestamp":1341964800000},"content-version":"vor","delay-in-days":192,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"funder":[{"name":"Funda\u00e7\u00e3o para a Ci\u00eancia e Tecnologia","award":["SFRH\/BD\/29712\/2006"],"award-info":[{"award-number":["SFRH\/BD\/29712\/2006"]}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Spectroscopy"],"published-print":{"date-parts":[[2012,1]]},"abstract":"<jats:p>The studies about the interaction of actin with vanadium are seldom. In the present paper the effects of vanadyl, vanadate, and decavanadate in the actin structure and function were compared. Decavanadate clearly interacts with actin, as shown by <jats:sub>\u2009<\/jats:sub><jats:sup>51<\/jats:sup>V\u2010NMR spectroscopy. Decavanadate interaction with actin induces protein cysteine oxidation and vanadyl formation, being both prevented by the natural ligand of the protein, ATP. Monomeric actin (G\u2010actin) titration with vanadyl, as analysed by EPR spectroscopy, indicates a 1\u2009:\u20091 binding stoichiometry and a <jats:italic>k<\/jats:italic><jats:sub>d<\/jats:sub> of 7.5\u2009<jats:italic>\u03bc<\/jats:italic>M. Both decavanadate and vanadyl inhibited G\u2010actin polymerization into actin filaments (F\u2010actin), with a IC<jats:sub>50<\/jats:sub> of 68 and 300\u2009<jats:italic>\u03bc<\/jats:italic>M, respectively, as analysed by light\u2010scattering assays. However, only vanadyl induces G\u2010actin intrinsic fluorescence quenching, which suggests the presence of vanadyl high\u2010affinity actin\u2010binding sites. Decavanadate increases (2.6\u2010fold) actin hydrophobic surface, evaluated using the ANSA probe, whereas vanadyl decreases it (15%). Finally, both vanadium species increased <jats:italic>\u03b5<\/jats:italic>\u2010ATP exchange rate (<jats:italic>k<\/jats:italic> = 6.5 \u00d7 10<jats:sup>\u22123<\/jats:sup> and 4.47 \u00d7 10<jats:sup>\u22123<\/jats:sup>\u2009s<jats:sup>\u22121<\/jats:sup> for decavanadate and vanadyl, resp.). Putting it all together, it is suggested that actin, which is involved in many cellular processes, might be a potential target not only for decavanadate but above all for vanadyl.<\/jats:p>","DOI":"10.1155\/2012\/532904","type":"journal-article","created":{"date-parts":[[2012,7,13]],"date-time":"2012-07-13T19:52:08Z","timestamp":1342209128000},"page":"355-359","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["A Comparison between Vanadyl, Vanadate, and Decavanadate Effects in Actin Structure and Function: Combination of Several Spectroscopic Studies"],"prefix":"10.1155","volume":"27","author":[{"given":"S.","family":"Ramos","sequence":"first","affiliation":[]},{"given":"J. J. 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