Discovery of a Multifunctional Octapeptide from Lingzhi with Antioxidant and Tyrosinase Inhibitory Activity
<i>Ganoderma lucidum</i> 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 pot...
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MDPI AG
2022-05-01
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| Series: | Pharmaceuticals |
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| Online Access: | https://www.mdpi.com/1424-8247/15/6/684 |
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| author | Yodying Yingchutrakul Sucheewin Krobthong Kiattawee Choowongkomon Phakorn Papan Pawitrabhorn Samutrtai Thanisorn Mahatnirunkul Thitikorn Chomtong Nitipol Srimongkolpithak Theeranuch Jaroenchuensiri Chanat Aonbangkhen |
| author_facet | Yodying Yingchutrakul Sucheewin Krobthong Kiattawee Choowongkomon Phakorn Papan Pawitrabhorn Samutrtai Thanisorn Mahatnirunkul Thitikorn Chomtong Nitipol Srimongkolpithak Theeranuch Jaroenchuensiri Chanat Aonbangkhen |
| author_sort | Yodying Yingchutrakul |
| collection | DOAJ |
| description | <i>Ganoderma lucidum</i> 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 NH<sub>2</sub>-PVRSSNCA-CO<sub>2</sub>H (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 FeSO<sub>4</sub>, 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. |
| first_indexed | 2024-03-09T22:47:06Z |
| format | Article |
| id | doaj.art-14a92b3dca574fc79fd8997f82a93cb1 |
| institution | Directory Open Access Journal |
| issn | 1424-8247 |
| language | English |
| last_indexed | 2024-03-09T22:47:06Z |
| publishDate | 2022-05-01 |
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| record_format | Article |
| series | Pharmaceuticals |
| spelling | doaj.art-14a92b3dca574fc79fd8997f82a93cb12023-11-23T18:26:58ZengMDPI AGPharmaceuticals1424-82472022-05-0115668410.3390/ph15060684Discovery of a Multifunctional Octapeptide from Lingzhi with Antioxidant and Tyrosinase Inhibitory ActivityYodying Yingchutrakul0Sucheewin Krobthong1Kiattawee Choowongkomon2Phakorn Papan3Pawitrabhorn Samutrtai4Thanisorn Mahatnirunkul5Thitikorn Chomtong6Nitipol Srimongkolpithak7Theeranuch Jaroenchuensiri8Chanat Aonbangkhen9National Omics Center, National Science and Technology Development Agency, Pathum Thani 12120, ThailandCenter for Neuroscience, Faculty of Science, Mahidol University, Bangkok 10400, ThailandInterdisciplinary Graduate Program in Genetic Engineering, Kasetsart University, Bangkok 10900, ThailandDepartment of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai 50200, ThailandDepartment of Pharmaceutical Sciences, Faculty of Pharmacy, Chiang Mai University, Chiang Mai 50200, ThailandNational Nanotechnology Center, National Science and Technology Development Agency, Pathum Thani 12120, ThailandNational Nanotechnology Center, National Science and Technology Development Agency, Pathum Thani 12120, ThailandNational Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathum Thani 12120, ThailandCenter of Excellence in Natural Products Chemistry (CENP), Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, ThailandCenter of Excellence in Natural Products Chemistry (CENP), Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand<i>Ganoderma lucidum</i> 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 NH<sub>2</sub>-PVRSSNCA-CO<sub>2</sub>H (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 FeSO<sub>4</sub>, 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.https://www.mdpi.com/1424-8247/15/6/684Lingzhibioactive peptidetyrosinase inhibitory peptideantioxidant peptideLC-MS/MSproteomics |
| spellingShingle | Yodying Yingchutrakul Sucheewin Krobthong Kiattawee Choowongkomon Phakorn Papan Pawitrabhorn Samutrtai Thanisorn Mahatnirunkul Thitikorn Chomtong Nitipol Srimongkolpithak Theeranuch Jaroenchuensiri Chanat Aonbangkhen Discovery of a Multifunctional Octapeptide from Lingzhi with Antioxidant and Tyrosinase Inhibitory Activity Pharmaceuticals Lingzhi bioactive peptide tyrosinase inhibitory peptide antioxidant peptide LC-MS/MS proteomics |
| title | Discovery of a Multifunctional Octapeptide from Lingzhi with Antioxidant and Tyrosinase Inhibitory Activity |
| title_full | Discovery of a Multifunctional Octapeptide from Lingzhi with Antioxidant and Tyrosinase Inhibitory Activity |
| title_fullStr | Discovery of a Multifunctional Octapeptide from Lingzhi with Antioxidant and Tyrosinase Inhibitory Activity |
| title_full_unstemmed | Discovery of a Multifunctional Octapeptide from Lingzhi with Antioxidant and Tyrosinase Inhibitory Activity |
| title_short | Discovery of a Multifunctional Octapeptide from Lingzhi with Antioxidant and Tyrosinase Inhibitory Activity |
| title_sort | discovery of a multifunctional octapeptide from lingzhi with antioxidant and tyrosinase inhibitory activity |
| topic | Lingzhi bioactive peptide tyrosinase inhibitory peptide antioxidant peptide LC-MS/MS proteomics |
| url | https://www.mdpi.com/1424-8247/15/6/684 |
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