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Last Updated: 3 years ago

Possible Interaction: Albumin and Warfarin

supplement:

Albumin

Research Papers that Mention the Interaction

For instance, albumin is able to bind long chain fatty acids, steroids, ions and various drugs, such as warfarin and ibuprofen [1].
Future medicinal chemistry  •  2015  |  View Paper
The fluorescent probes warfarin and dansylsarcosine are known to selectively interact with binding sites I and II, respectively, on human albumin.
Biochemical pharmacology  •  1992  |  View Paper
Certain agents, such as warfarin , that interact with the site I binding region of albumin reversed its stabilizing effect.
The Journal of biological chemistry  •  1982  |  View Paper
The procedure depends upon the enhancement of the fluorescence of warfarin when bound to albumin , and the diminution of fluorescence when drugs capable of displacing warfarin are added to the assay.
Toxicology and applied pharmacology  •  1975  |  View Paper
The overall results indicate that, under physiological condition, the binding of warfarin in site DS1 of albumin promotes local stabilization with resulting effects on the global protein dynamics.
Under denaturing condition, the stabilizing effect of warfarin is evidenced by an increase of both the melting temperature and unfolding enthalpy of albumin with the drug/protein molar ratio.
Archives of biochemistry and biophysics  •  2019  |  View Paper
The increase of albumin occurs rapidly after initiation of a high-protein diet and appears to promptly affect anticoagulation therapy with warfarin.
The Annals of pharmacotherapy  •  2005  |  View Paper
Numerous drugs such as warfarin , phenytoin or salicylates may displace chemotherapeutic agents from albumin binding sites (Spina and Scordo, 2002).
British Journal of Cancer  •  2004  |  View Paper
Flow microcalorimetry data demonstrated a decrease in the ability of uraemic albumin to bind octanoate, phenol red, salicylic acid, warfarin and diazepam.
Nephron Physiology  •  2003  |  View Paper
Both the warfarin and indole binding sites of albumin , the principal binding protein for these ligands, are affected.
Biochemical pharmacology  •  1985  |  View Paper
It is suggested that the availability of the binding sites for L-tryptophan, warfarin and salicylic acid is partially blocked by the complex between albumin and the dye without direct participation in the complex-formation.
The Biochemical journal  •  1983  |  View Paper
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