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Discovery of a Multifunctional Octapeptide from Lingzhi with Antioxidant and Tyrosinase Inhibitory Activity
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Document Title
Discovery of a Multifunctional Octapeptide from Lingzhi with Antioxidant and Tyrosinase Inhibitory Activity
Author
Yingchutrakul Y, Krobthong S, Choowongkomon K, Papan P, Samutrtai P, Mahatnirunkul T, Chomtong T, Srimongkolpithak N, Jaroenchuensiri T, Aonbangkhen C
Name from Authors Collection
Affiliations
National Science & Technology Development Agency - Thailand; Mahidol University; Kasetsart University; Chiang Mai University; Chiang Mai University; National Science & Technology Development Agency - Thailand; National Nanotechnology Center (NANOTEC); National Science & Technology Development Agency - Thailand; National Center Genetic Engineering & Biotechnology (BIOTEC); Chulalongkorn University
Type
Article
Source Title
PHARMACEUTICALS
Year
2022
Volume
15
Issue
6
Open Access
gold, Green Published
Publisher
MDPI
DOI
10.3390/ph15060684
Format
Abstract
Ganoderma lucidum or Lingzhi is a fungus species widely known as a traditional medicine. Exploring the beneficial peptides by hydrolysis using pepsin and trypsin has been extensively performed to identify new bioactive natural products. A multifunctional peptide that expresses potential scavenging activity and tyrosinase inhibition is valuable in therapeutic and cosmetic applications. This study aimed to identify and investigate the effects of a novel multifunctional peptide from Lingzhi on the melanogenic enzymes in melanoma cells by a targeted-proteomics approach. The multifunctional peptide was de novo sequenced by LC-MS/MS to be NH2-PVRSSNCA-CO2H (octapeptide). This sequence was chemically synthesized by solid-phase peptide synthesis (SPPS). The antioxidant ability of the synthesized octapeptide was measured by the DPPH, ABTS, and FRAP assays. The results showed that the peptide exhibited an antioxidant activity equal to 0.121 +/- 0.01 mg equivalent to ascorbic acid, 0.173 +/- 0.03 mg equivalent to gallic acid, and 2.21 +/- 0.23 mM equivalent to FeSO4, respectively, which is comparable to these well-known antioxidants. The proteomics approach identified a total of 5804 proteins and several pathways involved in the effects of the octapeptide in melanoma cells. Targeted proteomics revealed three specific proteins associated with pigmentation including Rab29, Dct, and Tyrp1. The Rab29 and Dct were upregulated whereas Tyrp1 was downregulated in the octapeptide treatment group. These findings could be used in the understanding of the molecular functions of the multifunctional octapeptide on melanogenic enzymes, supporting its potential as a therapeutic and cosmetic ingredient.
Industrial Classification
Knowledge Taxonomy Level 1
Knowledge Taxonomy Level 2
Knowledge Taxonomy Level 3
Funding Sponsor
Ratchadaphiseksomphot Endowment Fund from Chulalongkorn University [DNS 64_045_23_005_1]; Faculty of Science, Chulalongkorn University [Sci-Super VII_64_004]; Office of the Permanent Secretary, Ministry of Higher Education, Science, Research and Innovation [RGNS 64-004]; National Research Council of Thailand [NRCT5-RGJ63002-042]; Kasetsart University Research and Development Institute [FF (KU)6.64]
License
CC BY
Rights
Authors
Publication Source
WOS