title: Recognition and modulation of cytochrome c's redox properties using an amphiphilic homopolymer.
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.
authors.affiliation: Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA.
authors.forename: Britto S
authors.initials: BS
authors.lastname: Sandanaraj
authors.forename: Halil
authors.initials: H
authors.lastname: Bayraktar
authors.forename: Kothandam
authors.initials: K
authors.lastname: Krishnamoorthy
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Knapp
authors.forename: S
authors.initials: S
authors.lastname: Thayumanavan
mesh_terms: D045305:Cytochromes c' / Q000737:chemistry*; D010084:Oxidation-Reduction; D011108:Polymers / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D055672:Static Electricity
chemical_list: D045305:Cytochromes c'; D011108:Polymers