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It was found that the binding of PtCl(4) (2-) to G-actin and the consequent conformational changes are different with those for hard acids. It is a two-step process depending on molar ratio PtCl(4) (2-)/actin (R). In the first step, R less than 25, the PtCl(4) (2-) ions are bound to sulfur-containing groups preferentially. These high-affinity sites determined by Scatchard approach are characterized by n(1) = 30 with average binding constant K(1)=1.0x10(7)M(-1). The conformational changes are significant as characterized by N-(1-pyrenyl) maleimide(NPM) labeled fluorescence, intrinsic fluorescence and CD spectra. EPR spectroscopy of maleimide spin labeled(MSL) actin demonstrated that even PtCl(4) (2-)binding is limited to a very small fraction of high-affinity sites(R&lt;1), it can bring about a pronounced change of conformation. In the range of R=25-40, high-affinity sites accessible are saturated. In the second step(R&gt;40) , deep-buried binding sites turn out to be accessible as a result of the accumulated conformational changes. These new binding sites are estimated to be n(2)=26 with average binding constant K(2)=2.1x10(6)M(-1). Although in this step the quenching of intrinsic fluorescence goes on and the NPM-labled thiols moves to more hydrophilic environment, no change in alpha-helix content was found. These results suggested that with increasing in PtCl(4) ((2-)) binding, the G-actin turns to an open and loose structure in a discontinuous mode.

metal-based drugs

A Spectroscopic Study on <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" id="E1"><mml:msup><mml:mrow><mml:mo /><mml:mrow><mml:msub><mml:mrow><mml:mtext>PtCl</mml:mtext></mml:mrow><mml:mn>4</mml:mn></mml:msub></mml:mrow><mml:mo /></mml:mrow><mml:mrow><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mn>2</mml:mn><mml:mo>−</mml:mo></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow></mml:msup></mml:math> Binding to Rabbit Skeletal Muscle G-Actin

A Spectroscopic Study on PtCl4(2−) Binding to Rabbit Skeletal Muscle G-Actin