Applications of tailored ferrocenyl molecules as electrochemical probes of biochemical interactions.
The development of electrochemical probes useful for investigating the occupancy by other molecules of sites on complex proteins such as human serum albumin (HSA) is described. Ferrocenyl-(oxoethylene)-fatty acid compounds of different fatty acid chain length probed different binding sites on HSA. The interaction could be changed from one primarily with a drug binding site, when the probe was ferrocene methanol, to one predominantly with medium-chain fatty acid binding sites, by adding an (oxoethylene)-fatty acid substituents. Finally, the interaction could be changed to one interacting primarily with high-affinity long-chain fatty acid binding sites, as the fatty acid chain length in ferrocene-(oxoethylene)-fatty acid molecules increased. These results strongly implied that the binding could be further tailored by relatively simple modifications to the probe, for example, by changing the balance of hydrophobicity and hydrophilicity. The possibility of a procedure using mass-produced electrochemical cells to determine the fractional occupancy of different sites on HSA is demonstrated.
Tranchant
Isabelle
I
Department of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, UK.
Hervé
Anne-Cécile
AC
Carlisle
Stephen
S
Lowe
Phillip
P
Slevin
Christopher J
CJ
Forssten
Camilla
C
Dilleen
John
J
Tabor
Alethea B
AB
Williams
David E
DE
Hailes
Helen C
HC
D001669:Biochemical Phenomena; D001671:Biochemistry; D004563:Electrochemistry; D005296:Ferrous Compounds / Q000737:chemistry*; D006801:Humans; D000075163:Metallocenes; D015335:Molecular Probes / Q000737:chemistry*; D012709:Serum Albumin
D005296:Ferrous Compounds; D000075163:Metallocenes; D015335:Molecular Probes; D012709:Serum Albumin; C004998:ferrocene