2021
DOI: 10.1016/j.biopha.2021.111459
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Interaction of silymarin components and their sulfate metabolites with human serum albumin and cytochrome P450 (2C9, 2C19, 2D6, and 3A4) enzymes

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Cited by 13 publications
(9 citation statements)
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“…2 A and B). Since the interaction of ligand molecules with HSA causes a partial decrease in the emission signal of Trp214 in albumin, it is reasonable to hypothesize that MI-1851 does not interact with the protein or they form only poorly stable complexes [17] , [18] .
Fig.
…”
Section: Resultsmentioning
confidence: 99%
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“…2 A and B). Since the interaction of ligand molecules with HSA causes a partial decrease in the emission signal of Trp214 in albumin, it is reasonable to hypothesize that MI-1851 does not interact with the protein or they form only poorly stable complexes [17] , [18] .
Fig.
…”
Section: Resultsmentioning
confidence: 99%
“…The potential interaction of inhibitor MI-1851 with HSA was examined employing fluorescence quenching studies. Increasing amounts of MI-1851 (final concentrations: 0–10 μM) were added to HSA (2 μM) in phosphate-buffered saline (PBS, pH 7.4), after which the emission spectra were collected using 295 nm excitation wavelength [17] , [18] . Absorption spectra of MI-1851 in PBS was also recorded for the correction of the potential inner-filter effect, which was performed as it has been reported [17] , [18] .…”
Section: Methodsmentioning
confidence: 99%
“…53 In human plasma, avonolignans and their sulfated metabolites are mainly bound to a specic site of serum albumin. 63,64 Flavonolignans are metabolized predominantly via phase II reactions, i.e., conjugation (methylation, 65 sulfation, 66 glucuronidation, 67 and glutathione conjugation 68 64), (Fig. 11).…”
Section: Reviewmentioning
confidence: 99%
“…53 In human plasma, flavonolignans and their sulfated metabolites are mainly bound to a specific site of serum albumin. 63,64…”
Section: Pharmacokinetics Of Silymarin Flavonolignansmentioning
confidence: 99%
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