Hydrophobic interactions of phenoxazine modulators with bovine serum albumin |
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Authors: | H N Kalpana B C Channu Chhabil Dass P J Houghton and K N Thimmaiah |
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Institution: | (1) Department of Studies in Chemistry, University of Mysore, 570 006 Manasagangotri, Mysore, India;(2) Department of Chemistry, University of Memphis, TN 38151 Memphis, USA;(3) Department of Molecular Pharmacology, St. Jude Children’s Research Hospital, TN 38105 Memphis, USA |
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Abstract: | The interaction of 10-(3′-N-morpholinopropyl)phenoxazine MPP], 10-(4′-N-morpholinobutyl)phenoxazine MBP], 10-(3′-N-morpholinopropyl)-2-chlorophenoxazine
MPCP], 10-(3′-N-piperidinopropyl)-2-chlorophenoxazine PPCP] or 10-(3′-N-morpholinopropyl)-2-trifluoromethylphenoxazine MPTP]
with bovine serum albumin (BSA) has been studied by gel filtration and equilibrium dialysis methods. The binding of these
modulators, based on dialysis experiments, has been characterized using the following parameters: percentage of bound drug
(Β), the association constant (K
1), the apparent binding constant (k) and the free energy change (δF‡). The binding of phenoxazine derivatives to serum transporter protein, BSA, is correlated
with their octanol-water partition coefficient, log10
P. In addition, effect of the displacing activities of hydroxyzine and acetylsalicylic acid on the binding of phenoxazine derivatives
to albumin has been studied. Results of the displacement experiments show that phenoxazine benzene rings and tertiary amines
attached to the side chain of the phenoxazine moiety are bound to a hydrophobic area on the albumin molecule. |
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Keywords: | Phenoxazine hydrophobic interaction displacement experiments bovine serum albumin |
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