Interaction of substituted phenoxazine chemosensitizers with bovine serum albumin

Channu, B. C. and Kalpana, H. N. and Eregowda, G. B. and Dass, C. and Houghton, P. J. and Thimmaiah, K. N. (1999) Interaction of substituted phenoxazine chemosensitizers with bovine serum albumin. JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS, 21 (4). pp. 775-785.

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Official URL: http://dx.doi.org/10.1016/S0731-7085(99)00187-9

Abstract

The binding of 10-3'-N-bis(hydroxyethyl)amino]propyl]phenoxazine BPP], 10-3'-N-bis(hydroxyethyl)amino]propyl]-2-chlorophenoxazine BPCP], 10-3'-N-bis-(hydroxyethyl)amino]propyl]-2-trifluoromethylphenoxazi ne BPFP], 10-(3'-N-pyrrolidino propyl)-2-chlorophenoxazine PPCP] or 10-(3'-N-pyrrolidinopropyl)-2-trifluoromethylphenoxazine PPFP] to bovine serum albumin (BSA) has been measured by gel filtration and equilibrium dialysis methods. The binding of these modulators to bovine serum albumin based on dialysis experiments has been characterized by the following parameters: percentage (beta) of bound drug, the association constant `K-1', the apparent binding constant `k' and the free energy Delta F degrees. The binding of phenoxazine derivatives to bovine serum albumin is correlated with their octanol-water partition coefficient, log(10) P. In addition, the displacing activity of hydroxyzine and acetylsalicylic acid on the binding of phenoxazines to albumin has been studied. The results of the displacing experiments showed 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. (C) 1999 Elsevier Science B.V. All rights reserved.

Item Type: Article
Uncontrolled Keywords: phenoxazine; hydrophobic interaction; bovine serum albumin
Subjects: Physical Sciences > Chemistry
Divisions: PG Campuses > Manasagangotri, Mysore > Chemistry
Depositing User: Users 13 not found.
Date Deposited: 17 Apr 2013 08:48
Last Modified: 16 Aug 2013 06:51
URI: http://eprints.uni-mysore.ac.in/id/eprint/4724

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