Recognition and modulation of cytochrome c's redox properties using an amphiphilic homopolymer |
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Authors: | Sandanaraj Britto S Bayraktar Halil Krishnamoorthy Kothandam Knapp Michael J Thayumanavan S |
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Affiliation: | Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA. |
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Abstract: | An amphiphilic homopolymer scaffold has been used to bind to the protein, cytochrome c. This interaction is analyzed using cyclic voltammetry, native gel electrophoresis, UV-visible absorption, and circular dichroism spectroscopy. The polymer binds to cytochrome c with micromolar affinity and the association of polymer with cytochrome c leads to a structural change of the protein. This conformational change exposes the heme unit of the protein, which affords an opportunity to reversibly modulate its electron-transfer properties. We have also shown that the electrostatic binding of polymer to cytochrome c can be used to disrupt its interaction with its natural partner, cytochrome c peroxidase. |
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