Fluorescent investigations of binding of phenprocoumon to alpha 1-acid glycoprotein.

Article Details

Citation
Copy to clipboard

Otagiri M, Maruyama T, Imai T, Imamura Y

Fluorescent investigations of binding of phenprocoumon to alpha 1-acid glycoprotein.

J Pharm Sci. 1987 Aug;76(8):646-9.

PubMed ID
11002825 [ View in PubMed
]
Abstract

The fluorescence of phenprocoumon is greatly enhanced on binding to a single site on alpha 1-acid glycoprotein (alpha 1-AGP). Advantage is taken of this phenomenon to estimate a binding constant for the binding of phenprocoumon to alpha 1-AGP. The fluorescence intensity and binding constant of the phenprocoumon: alpha 1-AGP complex decreased with pH from 6.5 to 8.5, suggesting that phenprocoumon binding to alpha 1-AGP is significantly affected by microenvironmental change in alpha 1-AGP. A variety of drugs, including chlorpromazine and dicumarol, significantly inhibited phenprocoumon binding to alpha 1-AGP. Fatty acids seem to displace phenprocoumon from its binding site on alpha 1-AGP, whereas the addition of neutral salts and sialic acid did not cause the displacement of phenprocoumon. It is concluded that the phenprocoumon binding site is located in the hydrophobic protein structure of alpha 1-AGP.

DrugBank Data that Cites this Article

Drug Carriers
DrugCarrierKindOrganismPharmacological ActionActions
PhenprocoumonAlpha-1-acid glycoprotein 1ProteinHumans
No
Not AvailableDetails