Salicylate binding by human albumin in the presence of a perfluorochemical emulsion.
The binding of 43 and 216 micrograms/ml sodium salicylate by a perfluorochemical emulsion, by human albumin, and by their mixtures, has been examined at ambient room temperature. Sodium salicylate was chosen as a model drug since it is bound by both sites I and II on human albumin. The concentration of free salicylate was determined through standard centrifugation followed by supernatant ultrafiltration. Sodium salicylate was weakly bound by the perfluorochemical emulsion droplets through an interaction with the emulsifiers. This binding was independent of salicylate concentration. Sodium salicylate was also bound by human albumin and the per cent free salicylate was dependent on both drug and albumin concentration. Relative to salicylate binding by 4% human albumin, addition of the emulsion to 4% human albumin resulted in an increase in the per cent free salicylate in all mixtures examined. The addition of equal or greater volumes of the emulsion to 4% human albumin resulted in the direct and/or indirect displacement of albumin bound salicylate in addition to the protein dilution effect. This displacement of albumin bound salicylate was due to the oleic acid component of the emulsion.
Parsons
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DL
Department of Pharmacal Sciences, School of Pharmacy, Auburn University, AL 36849.
Sathe
R S
RS
D002498:Centrifugation; D004655:Emulsions; D005466:Fluorocarbons / Q000737:chemistry; D006801:Humans; D008024:Ligands; D011485:Protein Binding; D012459:Salicylates / Q000097:blood* / Q000737:chemistry; D020156:Salicylic Acid; D012709:Serum Albumin / Q000378:metabolism*; D014462:Ultrafiltration
D004655:Emulsions; D005466:Fluorocarbons; D008024:Ligands; D012459:Salicylates; D012709:Serum Albumin; D020156:Salicylic Acid