Original paper
Multi-spectroscopic and molecular docking technique study of the azelastine interaction with human serum albumin
Abstract
Fluorescence and circular dichroism spectroscopic techniques and molecular docking were used to study binding of azelastine with human serum albumin (HSA). Time resolve fluorescence spectroscopy results indicated that the quenching mechanism is dynamic. Fluorescence quenching results demonstrated that the binding of azelastine to HSA is weak, binding reaction is spontaneous. There is fluorescence energy transfer from tryptophan of HSA to bound...
Paper Details
Title
Multi-spectroscopic and molecular docking technique study of the azelastine interaction with human serum albumin
Published Date
Feb 1, 2020
Volume
1201
Pages
127147 - 127147
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Notes
History