Characterization of basic drug-human serum protein interactions by capillary electrophoresis.

Article Details

Citation

Martinez-Gomez MA, Sagrado S, Villanueva-Camanas RM, Medina-Hernandez MJ

Characterization of basic drug-human serum protein interactions by capillary electrophoresis.

Electrophoresis. 2006 Sep;27(17):3410-9. doi: 10.1002/elps.200600102.

PubMed ID
16944456 [ View in PubMed
]
Abstract

Drug-protein interactions are determining factors in the therapeutic, pharmacodynamic and toxicological drug properties. The affinity of drugs towards plasmatic proteins is apparently well established in bibliography. Albumin (HSA) especially binds neutral and negatively charged compounds; alpha(1)-acid glycoprotein (AGP) binds many cationic drugs, lipoproteins bind to nonionic and lipophilic drugs and some anionic drugs while globulins interact inappreciably with the majority of drugs. In this paper, the characterization of the interaction between cationic drugs, beta-blockers and phenotiazines towards HSA, AGP, and both HSA + AGP mixtures of proteins under physiological conditions by CE-frontal analysis is presented. Furthermore, the binding of these drugs to all plasmatic proteins is evaluated by using ultrafiltration and CE. The results indicate that the hydrophobic character of compounds seems to be the key factor on the interaction between cationic drugs towards proteins. In fact, hydrophobic basic drugs bind in great extension to HSA, while hydrophilic basic drugs present low interactions with proteins and bind especially to AGP.

DrugBank Data that Cites this Article

Drug Carriers
DrugCarrierKindOrganismPharmacological ActionActions
Labetalolalpha1-acid glycoprotein (Protein Group)Protein groupHumans
Unknown
Substrate
Details
LabetalolSerum albuminProteinHumans
Unknown
Substrate
Details