Unveiling the interaction profile of rosmarinic acid and its bioactive substructures with serum albumin.

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ID: 101323
2020
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Abstract
Rosmarinic acid, a phytochemical compound, bears diverse pharmaceutical profile. It is composed by two building blocks: caffeic acid and a salvianic acid unit. The interaction profile, responsible for the delivery of rosmarinic acid and its two substructure components by serum albumin remains unexplored. To unveil this, we established a novel low-cost and efficient method to produce salvianic acid from the parent compound. To probe the interaction profile of rosmarinic acid and its two substructure constituents with the different serum albumin binding sites we utilised fluorescence spectroscopy and competitive saturation transfer difference NMR experiments. These studies were complemented with transfer NOESY NMR experiments. The thermodynamics of the binding profile of rosmarinic acid and its substructures were addressed using isothermal titration calorimetry. docking studies, driven by the experimental data, have been used to deliver further atomic details on the binding mode of rosmarinic acid and its structural components.
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papaemmanouil2020unveilingjournal Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Papaemmanouil, Christina;Chatziathanasiadou, Maria V;Chatzigiannis, Christos;Chontzopoulou, Eleni;Mavromoustakos, Thomas;Grdadolnik, Simona Golic;Tzakos, Andreas G;
Journal Journal of enzyme inhibition and medicinal chemistry
Year 2020
DOI
10.1080/14756366.2020.1740923
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