Fluorescence Assay of Hydroxynaphthoquinones

Damme, Johan G. Van; Nève, R.e. De

doi:10.1002/jps.2600680109

Cited by 5 publications

(1 citation statement)

References 9 publications

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“…The resulting naphthoquinol is reoxidized to naphthoquinone by the O 2 in solution or by the unreacted shikonin molecules. This is also confirmed by the MS spectra (Δ m / z (Tyr 102 –Arg 124 ; Tyr 102 –Arg 124 –shikonin) ∼ 288 Da) and by the fact that shikonin is fluorescent in the reduced form, but shikonin failed to fluoresce under any circumstance even after its addition to the β-Lg.…”

Section: Resultssupporting

confidence: 60%

Addition of β-Lactoglobulin Produces Water-Soluble Shikonin

Albreht

Vovk

Simonovska

2012

J. Agric. Food Chem.

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Shikonin and its ester derivatives belong to a group of secondary metabolites with a wide array of beneficial effects on human health. However, shikonin is principally used in oil-based preparations due to the low solubility of the pigment in aqueous media, and the positive properties of shikonin are not exploited to their full potential. Such low aqueous solubility often results in poor bioavailability, makes shikonin undesirable for oral administration, and restricts its broadened use in the food and pharmaceutical industries. The purpose of this study was to enhance the aqueous solubility of shikonin by the addition of β-lactoglobulin and to characterize the macromolecule-ligand binding interaction by means of spectrophotometry, spectrofluorometry, high-performance liquid chromatography, and mass spectrometry. In the presence of β-lactoglobulin the solubility of shikonin is increased up to 181-fold. One shikonin molecule binds covalently to β-lactoglobulin via Cys(121), whereas the remaining pigment molecules most probably bind to the protein via noncovalent interactions.

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Section: Resultssupporting

confidence: 60%