Potency of bisresorcinol from Heliciopsis terminalis on skin aging: in vitro bioactivities and molecular interactions
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 a...
| Main Authors: | , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
PeerJ Inc.
2021-06-01
|
| Series: | PeerJ |
| Subjects: | |
| Online Access: | https://peerj.com/articles/11618.pdf |
| _version_ | 1797425777736679424 |
|---|---|
| author | Charinrat Saechan Uyen Hoang Nguyen Zhichao Wang Sachiko Sugimoto Yoshi Yamano Katsuyoshi Matsunami Hideaki Otsuka Giang Minh Phan Viet Hung Pham Varomyalin Tipmanee Jasadee Kaewsrichan |
| author_facet | Charinrat Saechan Uyen Hoang Nguyen Zhichao Wang Sachiko Sugimoto Yoshi Yamano Katsuyoshi Matsunami Hideaki Otsuka Giang Minh Phan Viet Hung Pham Varomyalin Tipmanee Jasadee Kaewsrichan |
| author_sort | Charinrat Saechan |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-09T08:21:07Z |
| format | Article |
| id | doaj.art-d59d9fb98cd846a4a7caf36aa72fb53b |
| institution | Directory Open Access Journal |
| issn | 2167-8359 |
| language | English |
| last_indexed | 2024-03-09T08:21:07Z |
| publishDate | 2021-06-01 |
| publisher | PeerJ Inc. |
| record_format | Article |
| series | PeerJ |
| spelling | doaj.art-d59d9fb98cd846a4a7caf36aa72fb53b2023-12-02T21:50:27ZengPeerJ Inc.PeerJ2167-83592021-06-019e1161810.7717/peerj.11618Potency of bisresorcinol from Heliciopsis terminalis on skin aging: in vitro bioactivities and molecular interactionsCharinrat Saechan0Uyen Hoang Nguyen1Zhichao Wang2Sachiko Sugimoto3Yoshi Yamano4Katsuyoshi Matsunami5Hideaki Otsuka6Giang Minh Phan7Viet Hung Pham8Varomyalin Tipmanee9Jasadee Kaewsrichan10Department of Pharmaceutical Chemistry and Drug Delivery System Excellence Center, Faculty of Pharmaceutical Sciences, Prince of Songkla University, Songkhla, ThailandGraduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, JapanGraduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, JapanGraduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, JapanGraduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, JapanGraduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, JapanFaculty of Pharmacy, Yasuda Women’s University, Hiroshima, JapanFaculty of Chemistry, VNU University of Science, Vietnam National University, Hanoi, VietnamResearch Center for Environmental Technology and Sustainable Development, VNU University of Science, Vietnam National University, Hanoi, VietnamDepartment of Biomedical Sciences and Biomedical Engineering, Faculty of Medicine, Prince of Songkla University, Songkhla, ThailandDepartment of Pharmaceutical Chemistry and Drug Delivery System Excellence Center, Faculty of Pharmaceutical Sciences, Prince of Songkla University, Songkhla, ThailandBackground 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.https://peerj.com/articles/11618.pdfHeliciopsis terminalisBisresorcinolCollagenaseElastaseTyrosinaseAnti-aging property |
| spellingShingle | Charinrat Saechan Uyen Hoang Nguyen Zhichao Wang Sachiko Sugimoto Yoshi Yamano Katsuyoshi Matsunami Hideaki Otsuka Giang Minh Phan Viet Hung Pham Varomyalin Tipmanee Jasadee Kaewsrichan Potency of bisresorcinol from Heliciopsis terminalis on skin aging: in vitro bioactivities and molecular interactions PeerJ Heliciopsis terminalis Bisresorcinol Collagenase Elastase Tyrosinase Anti-aging property |
| title | Potency of bisresorcinol from Heliciopsis terminalis on skin aging: in vitro bioactivities and molecular interactions |
| title_full | Potency of bisresorcinol from Heliciopsis terminalis on skin aging: in vitro bioactivities and molecular interactions |
| title_fullStr | Potency of bisresorcinol from Heliciopsis terminalis on skin aging: in vitro bioactivities and molecular interactions |
| title_full_unstemmed | Potency of bisresorcinol from Heliciopsis terminalis on skin aging: in vitro bioactivities and molecular interactions |
| title_short | Potency of bisresorcinol from Heliciopsis terminalis on skin aging: in vitro bioactivities and molecular interactions |
| title_sort | potency of bisresorcinol from heliciopsis terminalis on skin aging in vitro bioactivities and molecular interactions |
| topic | Heliciopsis terminalis Bisresorcinol Collagenase Elastase Tyrosinase Anti-aging property |
| url | https://peerj.com/articles/11618.pdf |
| work_keys_str_mv | AT charinratsaechan potencyofbisresorcinolfromheliciopsisterminalisonskinaginginvitrobioactivitiesandmolecularinteractions AT uyenhoangnguyen potencyofbisresorcinolfromheliciopsisterminalisonskinaginginvitrobioactivitiesandmolecularinteractions AT zhichaowang potencyofbisresorcinolfromheliciopsisterminalisonskinaginginvitrobioactivitiesandmolecularinteractions AT sachikosugimoto potencyofbisresorcinolfromheliciopsisterminalisonskinaginginvitrobioactivitiesandmolecularinteractions AT yoshiyamano potencyofbisresorcinolfromheliciopsisterminalisonskinaginginvitrobioactivitiesandmolecularinteractions AT katsuyoshimatsunami potencyofbisresorcinolfromheliciopsisterminalisonskinaginginvitrobioactivitiesandmolecularinteractions AT hideakiotsuka potencyofbisresorcinolfromheliciopsisterminalisonskinaginginvitrobioactivitiesandmolecularinteractions AT giangminhphan potencyofbisresorcinolfromheliciopsisterminalisonskinaginginvitrobioactivitiesandmolecularinteractions AT viethungpham potencyofbisresorcinolfromheliciopsisterminalisonskinaginginvitrobioactivitiesandmolecularinteractions AT varomyalintipmanee potencyofbisresorcinolfromheliciopsisterminalisonskinaginginvitrobioactivitiesandmolecularinteractions AT jasadeekaewsrichan potencyofbisresorcinolfromheliciopsisterminalisonskinaginginvitrobioactivitiesandmolecularinteractions |