Binding of alfentanil to human alpha 1-acid glycoprotein, albumin and serum.

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Belpaire FM, Bogaert MG

Binding of alfentanil to human alpha 1-acid glycoprotein, albumin and serum.

Int J Clin Pharmacol Ther Toxicol. 1991 Mar;29(3):96-102.

PubMed ID
2071261 [ View in PubMed
]
Abstract

The variability of the serum binding of the short-acting narcotic analgesic alfentanil was studied. Binding of alfentanil was measured in human alpha 1-acid glycoprotein (AAG) and human albumin solutions, and in serum from 6 groups of individuals: control subjects, patients with renal failure, cirrhosis, rheumatoid arthritis and myocardial infarction, and intensive care patients. Alfentanil is mainly bound to AAG and the influence of a change of the AAG concentration on its binding is much more marked than that of a change of the albumin concentration. In patients with renal failure, myocardial infarction and rheumatoid arthritis and in intensive care patients, AAG concentrations are increased, but alfentanil binding is significantly increased only in patients with myocardial infarction. In patients with cirrhosis, AAG, albumin concentrations, and alfentanil binding are decreased. In vitro addition of lidocaine, disopyramide, bupivacaine and quinidine, in concentrations that are observed clinically, lead only with disopyramide to an important increase in free fraction of alfentanil (from 7 to 19%). This latter finding was confirmed in 2 volunteers, treated chronically with disopyramide.

DrugBank Data that Cites this Article

Drug Carriers
DrugCarrierKindOrganismPharmacological ActionActions
AlfentanilAlpha-1-acid glycoprotein 1ProteinHumans
Unknown
Not AvailableDetails
AlfentanilSerum albuminProteinHumans
Unknown
Not AvailableDetails