6 alpha-Methylprednisolone and 6 alpha-methylprednisone plasma protein binding in humans and rabbits

The binding of 6 alpha-methylprednisolone and 6 alpha-methylprednisone to proteins of rabbit and human plasma was studied in vitro by equilibrium dialysis. Steroid binding was determined using radiolabeled compounds and HPLC analysis methods. Both methods produced equivalent results. Plasma protein...

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Bibliographic Details
Published inJournal of pharmaceutical sciences Vol. 75; no. 8; p. 760
Main Authors Ebling, W F, Milsap, R L, Szefler, S J, Jusko, W J
Format Journal Article
LanguageEnglish
Published United States 01.08.1986
Subjects
Animals
Blood Proteins - metabolism
Chromatography, High Pressure Liquid
Dialysis
Drug Stability
Humans
Methylprednisolone - blood
Prednisone - analogs & derivatives
Prednisone - blood
Protein Binding
Rabbits
Receptors, Steroid - metabolism
Species Specificity
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Summary:The binding of 6 alpha-methylprednisolone and 6 alpha-methylprednisone to proteins of rabbit and human plasma was studied in vitro by equilibrium dialysis. Steroid binding was determined using radiolabeled compounds and HPLC analysis methods. Both methods produced equivalent results. Plasma protein binding of 6 alpha-methylprednisolone and 6 alpha-methylprednisone averaged 75-82% and was independent of steroid concentration, suggestive of low affinity, nonspecific protein binding. A positive linear correlation of the log octanol-water partition coefficient with the nonspecific binding affinities of a homologous series of steroids, including 6 alpha-methylprednisolone and 6 alpha-methylprednisone, was demonstrated. This correlation suggests that hydrophobic binding is a major determinant of nonspecific steroid-protein interactions.
ISSN:0022-3549
DOI:10.1002/jps.2600750807