1Department of Chemistry, Faculty of Mathematics and Natural Sciences, IPB University, Bogor, Indonesia
2 Tropical Biopharmaca Research Center, IPB University, Bogor, Indonesia
BibTex Citation Data :
@article{JKSA61957, author = {Lutfia Mutmainnah and Irmanida Batubara and Auliya Ilmiawati}, title = {The Potency of Adenostemma platyphyllum as Antimelanogenic Agent: In-vitro and In-silico Studies}, journal = {Jurnal Kimia Sains dan Aplikasi}, volume = {27}, number = {5}, year = {2024}, keywords = {Asteraceae; docking; skin whitening; tyrosinase inhibition}, abstract = { Melanin is a crucial amino acid in determining human skin and hair pigmentation. Excessive melanin production can lead to hyperpigmentation and darkening of the skin. This study aims to assess the capability of Adenostemma platyphyllum as a tyrosinase enzyme inhibitor. It predicts its anti-melanogenic activity through molecular docking with proteins involved in the melanogenesis process. The in-vitro approach was conducted by determining the tyrosinase enzyme inhibition capacity, while the in-silico approach involved ligand binding to target proteins from melanogenesis pathways. The highest tyrosinase inhibition capacity was observed in the ethanol extract, with values of 9.74 Kojic Acid Equivalent (KAE)/g extract ( L- tyrosine) and 17.91 (KAE)/g extract ( L- DOPA). Molecular docking analysis showed that the binding of eriodictyol 7-O-sophoroside (ΔG = -9.7 kcal/mol) has the best energy affinity for the PKC-β protein, genistein (ΔG = -7.5 kcal/mol) for the tyrosinase-related protein-1 (TYRP1) protein, eriodictyol 7-O-sophoroside (ΔG = -10.2 kcal/mol) for the cGMP protein, vincosamide (ΔG = -7.2 kcal/mol) for the microphthalmia-associated transcription factor (MITF) protein, and dicaffeoylquinic acid (ΔG = -7.4 kcal/mol) for the β-catenin protein. Based on a comparison of in-vitro and in-silico studies, melanogenesis inhibition is more potent in the PKC-β and cGMP pathways than direct tyrosinase inhibition because they exhibit lower binding energy. }, issn = {2597-9914}, pages = {232--242} doi = {10.14710/jksa.27.5.232-242}, url = {https://ejournal.undip.ac.id/index.php/ksa/article/view/61957} }
Refworks Citation Data :
Melanin is a crucial amino acid in determining human skin and hair pigmentation. Excessive melanin production can lead to hyperpigmentation and darkening of the skin. This study aims to assess the capability of Adenostemma platyphyllum as a tyrosinase enzyme inhibitor. It predicts its anti-melanogenic activity through molecular docking with proteins involved in the melanogenesis process. The in-vitro approach was conducted by determining the tyrosinase enzyme inhibition capacity, while the in-silico approach involved ligand binding to target proteins from melanogenesis pathways. The highest tyrosinase inhibition capacity was observed in the ethanol extract, with values of 9.74 Kojic Acid Equivalent (KAE)/g extract (L-tyrosine) and 17.91 (KAE)/g extract (L-DOPA). Molecular docking analysis showed that the binding of eriodictyol 7-O-sophoroside (ΔG = -9.7 kcal/mol) has the best energy affinity for the PKC-β protein, genistein (ΔG = -7.5 kcal/mol) for the tyrosinase-related protein-1 (TYRP1) protein, eriodictyol 7-O-sophoroside (ΔG = -10.2 kcal/mol) for the cGMP protein, vincosamide (ΔG = -7.2 kcal/mol) for the microphthalmia-associated transcription factor (MITF) protein, and dicaffeoylquinic acid (ΔG = -7.4 kcal/mol) for the β-catenin protein. Based on a comparison of in-vitro and in-silico studies, melanogenesis inhibition is more potent in the PKC-β and cGMP pathways than direct tyrosinase inhibition because they exhibit lower binding energy.
Article Metrics:
Last update:
Last update: 2024-06-30 03:53:44
As an article writer, the author has the right to use their articles for various purposes, including use by institutions that employ authors or institutions that provide funding for research. Author rights are granted without special permission.
Author who publishes a paper at JKSA has the broad right to use their work for teaching and scientific purposes without the need to ask permission, including: used for (i) teaching in the author's class or institution, (ii) presentation at meetings or conferences and distributing copies to participants ; (iii) training conducted by the author or author's institution; (iv) distribution to colleagues for research use; (v) use in the compilation of subsequent authors' works; (vi) inclusion in a thesis or dissertation; (vi) reuse of part of the article in another work (with citation); (vii) preparation of derivative works (with citation); (viii) voluntary posting on open websites operated by authors or author institutions for scientific purposes (follow the CC BY-SA License).
Authors and readers can copy and redistribute material in any media or format, and mix, modify, and build material for any purpose but they must provide appropriate credit (provide article citation or content), providing links to the license, and indicate if there are changes.
The authors submitting a manuscript do so on the understanding that if accepted for publication, copyright of the article shall be assigned to Jurnal Kimia Sains dan Aplikasi (JKSA). Copyright encompasses rights to reproduce and deliver the article in all form and media, including reprints, photographs, microfilms and any other similar reproductions, as well as translations.
Reproduce any part of this journal, its storage in the database or its transmission by all forms or media is permitted does not need for written permission from JKSA. However, it should be cited as an honor in academic manners
JKSA and the Chemistry Department of Diponegoro University and the Editor make every effort to ensure that there are no data, opinions, or false or misleading statements published in JKSA. However, the content of the article is the sole and exclusive responsibility of each author.
The Copyright Transfer Form can be downloaded here: [Copyright Transfer Form - Indonesian] [Copyright Transfer Form - English]. The copyright form should be signed originally and send to the Editor in the form of printed letters, scanned documents sent via email or fax.
Adi Darmawan, Ph.D (Editor in Chief)
Editor in chief of Jurnal Kimia Sains dan Aplikasi (JKSA)
Chemistry Department, Faculty of Sciences and Mathematics, Diponegoro University
Visitor: View My Stats
Jurnal Kimia Sains dan Aplikasi is indexed in:
This work is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.
