Synthesis and electrochemical characterization of a transition-metal-modified ligand-receptor pair.
The energetics of weak interactions (van der Waals forces, hydrogen bonding) are difficult to quantify in biological ligand-receptor pairs. Insight into the biochemical role these forces play is critical to an understanding of signal transduction events and the drug discovery process. Ruthenium pentaammine and iron tetracyano complexes modified with either biotin or desthiobiotin have been synthesized and characterized. These modified biological ligands bind to the protein avidin in a manner similar to that of native biotin. Experiments using redox mediators show that the avidin-bound complexes are electrochemically accessible.
Eckermann
Amanda L
AL
Department of Chemistry, Northwestern University, 2145 North Sheridan Road, Evanston, Illinois 60208, USA.
Barker
Kylie D
KD
Hartings
Matthew R
MR
Ratner
Mark A
MA
Meade
Thomas J
TJ
D001360:Avidin / Q000737:chemistry / Q000378:metabolism; D001710:Biotin / Q000737:chemistry / Q000378:metabolism; D004563:Electrochemistry; D005290:Ferric Compounds / Q000138:chemical synthesis; D005296:Ferrous Compounds / Q000138:chemical synthesis; D008024:Ligands; D008670:Metals / Q000737:chemistry*; D015394:Molecular Structure; D009942:Organometallic Compounds / Q000138:chemical synthesis*; D011506:Proteins / Q000737:chemistry; D017975:Ruthenium Compounds / Q000138:chemical synthesis; D028561:Transition Elements / Q000737:chemistry*
D005290:Ferric Compounds; D005296:Ferrous Compounds; D008024:Ligands; D008670:Metals; D009942:Organometallic Compounds; D011506:Proteins; D017975:Ruthenium Compounds; D028561:Transition Elements; D001360:Avidin; D001710:Biotin