文摘
The development of electrochemical probes useful for investigating the occupancy by other molecules of sites oncomplex proteins such as human serum albumin (HSA) is described. Ferrocenyl-(oxoethylene)-fatty acid compoundsof different fatty acid chain length probed different binding sites on HSA. The interaction could be changed fromone 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 bechanged to one interacting primarily with high-affinity long-chain fatty acid binding sites, as the fatty acid chainlength in ferrocene-(oxoethylene)-fatty acid molecules increased. These results strongly implied that the bindingcould be further tailored by relatively simple modifications to the probe, for example, by changing the balanceof hydrophobicity and hydrophilicity. The possibility of a procedure using mass-produced electrochemical cellsto determine the fractional occupancy of different sites on HSA is demonstrated.