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Last Updated: 2 years ago

Possible Interaction: Chlorogenic Acid and Serum Albumin, Human

Research Papers that Mention the Interaction

The molecular docking and fluorescence spectroscopy demonstrate that CGA had a static quenching effect on rHSA with one binding site, and the range of K values was 7.14 × 103 to 1.56 × 104 M-1.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences  •  2019  |  View Paper
CCA presented the strongest ability of hydrogen-bond formation, and both CA and NCA generated more electrostatic interactions with HSA.
Food chemistry  •  2016  |  View Paper
Site marker competitive displacement experiments demonstrated that CGA specific bind to site I (subdomain IIA) of HSA.
Molecular Biology Reports  •  2011  |  View Paper
Binding of chlorogenic acid induces conformational change in HSA as indicated by quenching of fluorescence emission intensity along with a red shift in the emission maxima from 338 to 350 nm.
Far-ultraviolet circular dichroic data showed a decrease in the alpha-helical content of HSA from 56 to 50% upon binding of CGA.
These data are also supported by the decrease in the apparent Tm of HSA by 4 degrees C upon binding of CGA causing destabilization of the HSA molecule.
These high Ka-values showed that the interaction between CGA and HSA is strong, endothermic and entropically driven.
International journal of peptide and protein research  •  1995  |  View Paper