Please use this identifier to cite or link to this item: http://nopr.niscpr.res.in/handle/123456789/16733
Title: Hydrophobic interactions of phenoxazine MDR modulators with bovine serum albumin
Authors: Eregowda, G B
Channu, B C
Jagadeesh, S
Kalpana, H N
Hegde, Ravi
Houghton, P J
Thimmaiah, K N
Issue Date: Sep-2000
Publisher: NISCAIR-CSIR, India
Abstract: The binding of 10-[3'-(N-piperidino)propyl]-2-trifluoromethylphenoxazine 1, 10-[3'-(β-hydroxyethylpiperazino)-propyl]-2-trifluoromethylphenoxazine 2,10-[4'-(N-diethylamino)butyl]-2-trifluoromethylphenoxazine 3, 10-[4'-(N-piper-idino) 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 (β), the association constant (K1), the apparent binding constant (k) and the free energy (ΔFo). 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.
Page(s): 680-687
ISSN: 0975-0983(Online); 0376-4699(Print)
Appears in Collections:IJC-B Vol.39B(09) [September 2000]

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