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Interaction of loratadine with serum albumins studied by fluorescence quenching method

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DOI: 10.1016/j.jbbm.2007.04.001

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loratadine; fluorescence quenching; tryptophan; serum albumin

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The interactions between loratadine and bovine serum albumin (BSA) and human serum albumin (HSA) were studied using tryptophan fluorescence quenching method. The fluorescence intensity of the two serum albumins could be quenched 70% at the molar ratio [loratadine]: [BSA (or HSA)]= 10: 1. In the linear range (0-50 mu mol L-1) quenching constants were calculated using Stem-Volmer equation. Temperature in the range 298 K-310 K had a significant effect (p<0.05) on the two serum albumins through ANOVA analysis and t-test. Furthermore the conformation changes in the interactions were studied using FTIR spectroscopy. (c) 2007 Elsevier B.V. All rights reserved.

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