Abstract
BackgroundA bisresorcinol was isolated as the main constituent of Heliciopsis terminalis’s trunk (Proteaceae). Recently, resorcinol is applied as an active whitening agent in various cosmetic products. Because of the structural mimic to resorcinol, benefits of the bisresorcinol as an aging-enzyme antagonist were demonstrated in this study.MethodsThe bisresorcinol was purified from the crude ethanolic extract of H. terminalis’s trunk by solvent extraction and preparative chromatography, respectively. Inhibitory activity on collagenase, elastase, and tyrosinase of the compound was investigated by using a different spectroscopic technique. Molecular docking was carried out to predict possible interactions of the substance around the enzyme active sites.ResultsThe IC50 values on collagenase of the bisresorcinol and caffeic acid were 156.7 ± 0.7 and 308.9 ± 1.6 µmole L−1, respectively. For elastase activity, the IC50 of 33.2 ± 0.5 and 34.3 ± 0.3 µmole L−1 was respectively determined for the bisresorcinol and ursolic acid. The bisresorcinol was inhibitory to tyrosinase by exhibiting the IC50 of 22.8 µmole L−1, and that of 78.4 µmole L−1 was present for β-arbutin. The bisresorcinol bound to collagenase, elastase, and tyrosinase with the respective binding energies of −5.89, −5.69, and −6.57 kcal mol−1. These binding energies were in the same ranges of tested inhibitors. The aromatic phenol groups in the structure were responsible for principle as well as supporting binding interactions with enzymes. Hydrogen binding due to hydroxyl groups and π-related attractive forces from an aromatic ring(s) provided binding versatility to bisresorcinol.ConclusionThe bisresorcinol purified from H. terminalis might be useful for inclusion in cosmetic products as an aging-enzyme antagonist.
Highlights
A bisresorcinol, (8′Z)-3,5-dihydroxy-1-[16′-(3′′,5′′-dihydroxyphenyl)-8′-hexadecen-1′-yl] benzene, has been isolated as an abundant constituent from the trunk of Heliciopsis terminalis (Kurz) Sleumer, which is a plant of Proteaceae family and has been used by ethnic people in Vietnam for hepatoprotective effect
Compounds that can form complexes with metal ions are anticipated to be inhibitory to collagenases, elastases, and tyrosinase (Selvaraj et al, 2014). This project aims to determine biological effects of the bisresorcinol on tyrosinase, collagenase, and elastase in vitro, and docking technique was carried out to clarify their interactions at molecular levels
Hydrophobic interactions that occurred between phenolic hydroxyl groups and amino acid residues at/nearby the enzyme active sites might be contributors for loss of enzyme functions, consisting with the previous literatures
Summary
A bisresorcinol, (8′Z)-3,5-dihydroxy-1-[16′-(3′′,5′′-dihydroxyphenyl)-8′-hexadecen-1′-yl] benzene, has been isolated as an abundant constituent from the trunk of Heliciopsis terminalis (Kurz) Sleumer, which is a plant of Proteaceae family and has been used by ethnic people in Vietnam for hepatoprotective effect. Various synthetic and natural compounds with distinct chemical structures have been demonstrated to exhibit anti-tyrosinase activity (Dobos et al, 2015). Resorcinol is applied as an active whitening agent in various cosmetic products. Because of the structural mimic to resorcinol, benefits of the bisresorcinol as an aging-enzyme antagonist were demonstrated in this study. The bisresorcinol bound to collagenase, elastase, and tyrosinase with the respective binding energies of −5.89, −5.69, and −6.57 kcal mol−1. These binding energies were in the same ranges of tested inhibitors. Conclusion: The bisresorcinol purified from H. terminalis might be useful for inclusion in cosmetic products as an aging-enzyme antagonist
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