Hydrophobic interactions of phenoxazine MDR modulators with bovine serum albumin

Eregowda, G. B. and Channu, B. C. and Jagadeesh, S. and Kalpana, H. N. and Hegdekatte, R. and Houghton, P. J. and Thimmaiah, K. N. (2000) Hydrophobic interactions of phenoxazine MDR modulators with bovine serum albumin. Indian Journal of Chemistry Section B-Organic Chemistry Including Medicinal Chemistry, 39 (9). pp. 680-687. ISSN 0376-4699

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Abstract

The binding of 10-3'-(N-piperidino)propyl]-2-trifluoromethy]phenoxazine 1, 10- 3'-(beta -hydroxyethylpiperazino)propyl]-2-trifluoromethylphenoxazine 2, 10-4'-(N-diethylamino)butyl]-2-trifluoromethylphenoxazine 3, 10-4'-(N-piperidino)butyl]-2-trifluoromethylphenoxazine 4 and 10-4'-(N-diethylamino)butyl]-2-chlorophenoxazine 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 (beta), the association constant (K-I), the apparent binding constant (k) and the free energy (DeltaF degrees). 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.

Item Type:	Article
Subjects:	C Chemical Science > Chemistry
Divisions:	Department of > Chemistry
Depositing User:	Users 19 not found.
Date Deposited:	23 Sep 2019 05:39
Last Modified:	23 Sep 2019 05:39
URI:	http://eprints.uni-mysore.ac.in/id/eprint/8346

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