Specific vectorial immobilization of oligonucleotide-modified yeast cytochrome C on carbon nanotubes.
Iso-1-cytochrome c from the yeast Saccharomyces cerevisiae (YCC) contains a surface cysteine residue, Cys102, that is located opposite to the lysine-rich side containing the exposed heme edge, which is the docking site for enzymes. Site-specific vectorial immobilization of YCC via Cys102 on single-walled carbon nanotubes (SWNT) thus provides a selective interface between nanoscopic electronic devices and complex enzymes. We have achieved this by modification of Cys102 with an oligonucleotide (dT(18)). Atomic force microscopy, fluorescence imaging, and cyclic voltammetry show the specific adsorption of YCC, modified with dT(18), on the SWNT sidewall with retention of its native properties. Pretreatment of the SWNT with Triton-X405 blocks the nonspecific binding of untreated YCC but does not interfere with binding of the oligonucleotide-modified YCC.
Heering
Hendrik A
HA
Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC Leiden, The Netherlands. h.a.heering@chem.leidenuniv.nl
Williams
Keith A
KA
de Vries
Simon
S
Dekker
Cees
C
D000327:Adsorption; D001665:Binding Sites; D015374:Biosensing Techniques; D003545:Cysteine / Q000737:chemistry; D045304:Cytochromes c / Q000737:chemistry*; D003902:Detergents / Q000494:pharmacology; D004563:Electrochemistry / Q000379:methods; D004798:Enzymes / Q000737:chemistry; D008239:Lysine / Q000737:chemistry; D018625:Microscopy, Atomic Force; D008856:Microscopy, Fluorescence; D037742:Nanotubes, Carbon / Q000737:chemistry*; D009841:Oligonucleotides / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013053:Spectrophotometry
D003902:Detergents; D004798:Enzymes; D037742:Nanotubes, Carbon; D009841:Oligonucleotides; D045304:Cytochromes c; D008239:Lysine; D003545:Cysteine