Hydrophobic interactions of phenoxazine MDR modulators with bovine serum albumin

G. B. Eregowda, B. C. Channu, S. Jagadeesh, H. N. Kalpana, R. Hegde, P. J. Houghton, K. N. Thimmaiah

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The binding of 10-[3'-(N-piperidino)propyl]-2-trifluoromethylphenoxazine 1, 10-[3'-(β-hydroxyethylpiperazino)propyl]-2-trifluoromethylph enoxazine 2, 10-[4'-(N-diethylamino)butyl]-2-trifluoromethylphenoxazine 3, 10-[4'-(N-piperidino)butyl]-2-trifluoromethylphenoxazine 4 and 10-[4'-(N-diethylamino)butyl]-2-chlorophenoxazíne 5 to bovine serum albumin (BSA) has been measured by gel filtration and equilibrium dialysis methods. The binding of these modulators to albumin has been characterized by the following parameters: percentage of bound drug (β), the association constant (K1), the apparent binding constant (k) and the free energy (AF°). In addition, the displacing activity of hydroxyzine and acetylsalicylic acid on the binding of phenoxazine to albumin has been examined. The binding of phenoxazine derivatives to serum transporter protein, BSA, is correlated with their partition coefficients. The results of the displacing experiments reveal that the phenoxazine benzene rings and the tertiary amines attached to the side chain of the phenoxazine moiety are bound to a hydrophobic area on the albumin molecule.

Original languageEnglish (US)
Pages (from-to)680-687
Number of pages8
JournalIndian Journal of Chemistry - Section B Organic and Medicinal Chemistry
Volume39
Issue number9
StatePublished - Dec 1 2000
Externally publishedYes

ASJC Scopus subject areas

  • Pharmacology, Toxicology and Pharmaceutics(all)
  • Organic Chemistry

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