ArticleJournal of enzyme inhibition and medicinal chemistry2020
Unveiling the interaction profile of rosmarinic acid and its bioactive substructures with serum albumin.
Article in Journal of enzyme inhibition and medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Probing the biological efficacy and mechanistic pathways of natural compounds in breast cancer therapy via the Hedgehog signaling pathway.Journal of pharmaceutical analysis · 2025Review
- Synthesis of Anti-Inflammatory Drugs' Chalcone Derivatives and a Study of Their Conformational Properties Through a Combination of Nuclear Magnetic Resonance Spectroscopy and Molecular Modeling.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Analyzing Amylin Aggregation Inhibition Through Quantum Dot Fluorescence Imaging.International journal of molecular sciences · 2024Article
- Molecular mechanism of FeProtein science : a publication of the Protein Society · 2024Article
- Detecting and Characterizing Interactions of Metabolites with Proteins by Saturation Transfer Difference Nuclear Magnetic Resonance (STD NMR) Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Sensitive Detection of Rosmarinic Acid Using Peptide-Modified Graphene Oxide Screen-Printed Carbon Electrode.Nanomaterials (Basel, Switzerland) · 2022Article
- New systematic study approach of green synthesis CdS thin film via Salvia dye.Scientific reports · 2022Article
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Authors and funding
7 authors.
Funding
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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.
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