Potency of bisresorcinol from Heliciopsis terminalis on skin aging: in vitro bioactivities and molecular interactions

Abstract

Background A 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. Methods The 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. Results The 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. Conclusion The bisresorcinol purified from H. terminalis might be useful for inclusion in cosmetic products as an aging-enzyme antagonist.

Submerged fermentation with Lactobacillus brevis significantly improved the physiological activities of Citrus aurantium flower extract

“…In addition, gallic acid is an effective inhibitor of collagenase, elastase, and MMP-2 activity ( Wittenauer et al., 2015 ; Poomanee et al., 2021 ). Caffeic acid has been found to be an effective inhibitor of collagenase and MMP-1 activity ( Shin et al., 2019 ; Saechan et al., 2021 ), and neohesperidin reduces MMP-1 activity ( Karim et al., 2021 ). Naringin has been discovered to significantly inhibit the production of elastase or downregulate MMP-2 expression ( Annapoorani et al., 2012 ; Aroui et al., 2016 ).…”

Exploring Major Flavonoid Phytochemicals from Nelumbo nucifera Gaertn. as Potential Skin Anti-Aging Agents: In Silico and In Vitro Evaluations

“…This interaction likely disrupts the binding with the catalytic Zn 2+ during catalysis, thereby inhibiting the The critical residues in collagenase that participated in binding with Kae-3-Rob included N492, G493, G494, R508, F515, L520, E555, E559, D603, and W604. These stabilizing amino acid residues were also implicated in the binding of other reported collagenase inhibitors such as ohioensin A, nor-ohioensin D [46], bisresorcinol [47], and turmerone [48]. Notably, residue E555, which is one of the Zn 2+ -binding residues, exhibited the most negative energy contribution (∆G res bind of −6.9 kcal/mol) to ligand binding, primarily through electrostatic interactions (as discussed later in Figure 6).…”

Anticancer mechanism of 7-α-hydroxyfrullanolide on microtubules and computational prediction of its target binding in triple-negative breast cancer cells

“…Molecular docking was done to predict whether 7HF bound to the target protein, as per a previous study with certain modifications ( Saechan et al, 2021 ). The PDB ascension number 5SYF represents the three-dimensional (3D) protein structure of α-, β-tubulin ( Kellogg et al, 2017 ).…”