4.6 Article

Proteo-dendrimers designed for complementary recognition of cytochrome c:: Dendrimer architecture toward nanoscale protein complexation

Journal

CHEMISTRY-A EUROPEAN JOURNAL
Volume 12, Issue 5, Pages 1328-1338

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.200501131

Keywords

cytochromes; dendrimers; fluorescence; protein recognition; supramolecular chemistry

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Proteo-dendrimers in which polyanionic hepta(glutamic acids), fluorescent zinc porphyrinate cores, hydrophilic polyether surfaces, and nonpeptide hydrophobic dendrons are combined, were developed as a new series of synthetic receptors for protein recognition. They have polyanionic patch structures on their surfaces and undergo complementary electrostatic interactions with a positively charged cytochrome c patch, as observed in biological protein-protein recognition systems. Stability constants of the resulting supramolecular complexes were determined in phosphate buffer (pH 7) by monitoring the fluorescence quenching of the zinc porphyrinates. These proteo-dendrimer receptors exhibited higher affinities with cytochrome c proteins in aqueous solutions than with biological cytochrome b(5). Furthermore, they effectively blocked complexation of biological cytochrome b(5) with cytochrome c, indicating that the proteo-dendrimers and cytochrome b(5) similarly occupy the polycationic patch of cytochrome c.

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