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

PeerJ

article

Charinrat Saechan¹  Uyen Hoang Nguyen²  Zhichao Wang²  Sachiko Sugimoto²  Yoshi Yamano²  Katsuyoshi Matsunami²  Hideaki Otsuka³  Giang Minh Phan⁴  Viet Hung Pham⁵  Varomyalin Tipmanee⁶  Jasadee Kaewsrichan¹ 

[1] Department of Pharmaceutical Chemistry and Drug Delivery System Excellence Center, Faculty of Pharmaceutical Sciences, Prince of Songkla University;Graduate School of Biomedical and Health Sciences, Hiroshima University;Faculty of Pharmacy, Yasuda Women’s University;Faculty of Chemistry, VNU University of Science, Vietnam National University;Research Center for Environmental Technology and Sustainable Development, VNU University of Science, Vietnam National University;Department of Biomedical Sciences and Biomedical Engineering, Faculty of Medicine, Prince of Songkla University

关键词: Heliciopsis terminalis;    Bisresorcinol;    Collagenase;    Elastase;    Tyrosinase;    Anti-aging property;    Molecular docking;    Enzyme inhibition;   

DOI  :  10.7717/peerj.11618

学科分类：社会科学、人文和艺术（综合）

来源: Inra

【 摘 要 】

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.

【 授权许可】

CC BY