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Proteo‐Dendrimers Designed for Complementary Recognition of Cytochrome c : Dendrimer Architecture toward Nanoscale Protein Complexation
Author(s) -
Paul Dharam,
Miyake Hiroyuki,
Shinoda Satoshi,
Tsukube Hiroshi
Publication year - 2006
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200501131
Subject(s) - dendrimer , nanoscopic scale , cytochrome c , architecture , molecular recognition , chemistry , cytochrome , nanotechnology , materials science , molecule , biochemistry , enzyme , organic chemistry , mitochondrion , art , visual arts
“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 .