Antamanide Analogs as Potential Inhibitors of Tyrosinase
The tyrosinase enzyme, which catalyzes the hydroxylation of monophenols and the oxidation of <i>o</i>-diphenols, is typically involved in the synthesis of the dark product melanin starting from the amino acid tyrosine. Contributing to the browning of plant and fruit tissues and to the hy...
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MDPI AG
2022-06-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/11/6240 |
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| author | Claudia Honisch Matteo Gazziero Roberto Dallocchio Alessandro Dessì Davide Fabbri Maria Antonietta Dettori Giovanna Delogu Paolo Ruzza |
| author_facet | Claudia Honisch Matteo Gazziero Roberto Dallocchio Alessandro Dessì Davide Fabbri Maria Antonietta Dettori Giovanna Delogu Paolo Ruzza |
| author_sort | Claudia Honisch |
| collection | DOAJ |
| description | The tyrosinase enzyme, which catalyzes the hydroxylation of monophenols and the oxidation of <i>o</i>-diphenols, is typically involved in the synthesis of the dark product melanin starting from the amino acid tyrosine. Contributing to the browning of plant and fruit tissues and to the hyperpigmentation of the skin, leading to melasma or age spots, the research of possible tyrosinase inhibitors has attracted much interest in agri-food, cosmetic, and medicinal industries. In this study, we analyzed the capability of antamanide, a mushroom bioactive cyclic decapeptide, and some of its glycine derivatives, compared to that of pseudostellarin A, a known tyrosinase inhibitor, to hinder tyrosinase activity by using a spectrophotometric method. Additionally, computational docking studies were performed in order to elucidate the interactions occurring with the tyrosinase catalytic site. Our results show that antamanide did not exert any inhibitory activity. On the contrary, the three glycine derivatives <b>AG9</b>, <b>AG6</b>, and <b>AOG9</b>, which differ from each other by the position of a glycine that substitutes phenylalanine in the parent molecule, improving water solubility and flexibility, showed tyrosinase inhibition by spectrophotometric assays. Analytical data were confirmed by computational studies. |
| first_indexed | 2024-03-10T01:14:42Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T01:14:42Z |
| publishDate | 2022-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-f4d5fa36ae2a4e8f8c1d2cb013b0abc22023-11-23T14:12:16ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-06-012311624010.3390/ijms23116240Antamanide Analogs as Potential Inhibitors of TyrosinaseClaudia Honisch0Matteo Gazziero1Roberto Dallocchio2Alessandro Dessì3Davide Fabbri4Maria Antonietta Dettori5Giovanna Delogu6Paolo Ruzza7Institute of Biomolecular Chemistry of CNR, Padova Unit, Via F. Marzolo, 1, 35131 Padova, ItalyInstitute of Biomolecular Chemistry of CNR, Padova Unit, Via F. Marzolo, 1, 35131 Padova, ItalyInstitute of Biomolecular Chemistry of CNR, Sassari Unit, Traversa La Crucca, 3, 07100 Sassari, ItalyInstitute of Biomolecular Chemistry of CNR, Sassari Unit, Traversa La Crucca, 3, 07100 Sassari, ItalyInstitute of Biomolecular Chemistry of CNR, Sassari Unit, Traversa La Crucca, 3, 07100 Sassari, ItalyInstitute of Biomolecular Chemistry of CNR, Sassari Unit, Traversa La Crucca, 3, 07100 Sassari, ItalyInstitute of Biomolecular Chemistry of CNR, Sassari Unit, Traversa La Crucca, 3, 07100 Sassari, ItalyInstitute of Biomolecular Chemistry of CNR, Padova Unit, Via F. Marzolo, 1, 35131 Padova, ItalyThe tyrosinase enzyme, which catalyzes the hydroxylation of monophenols and the oxidation of <i>o</i>-diphenols, is typically involved in the synthesis of the dark product melanin starting from the amino acid tyrosine. Contributing to the browning of plant and fruit tissues and to the hyperpigmentation of the skin, leading to melasma or age spots, the research of possible tyrosinase inhibitors has attracted much interest in agri-food, cosmetic, and medicinal industries. In this study, we analyzed the capability of antamanide, a mushroom bioactive cyclic decapeptide, and some of its glycine derivatives, compared to that of pseudostellarin A, a known tyrosinase inhibitor, to hinder tyrosinase activity by using a spectrophotometric method. Additionally, computational docking studies were performed in order to elucidate the interactions occurring with the tyrosinase catalytic site. Our results show that antamanide did not exert any inhibitory activity. On the contrary, the three glycine derivatives <b>AG9</b>, <b>AG6</b>, and <b>AOG9</b>, which differ from each other by the position of a glycine that substitutes phenylalanine in the parent molecule, improving water solubility and flexibility, showed tyrosinase inhibition by spectrophotometric assays. Analytical data were confirmed by computational studies.https://www.mdpi.com/1422-0067/23/11/6240tyrosinase inhibitionantamanidebioactive peptidesUV-spectroscopycomputational docking |
| spellingShingle | Claudia Honisch Matteo Gazziero Roberto Dallocchio Alessandro Dessì Davide Fabbri Maria Antonietta Dettori Giovanna Delogu Paolo Ruzza Antamanide Analogs as Potential Inhibitors of Tyrosinase International Journal of Molecular Sciences tyrosinase inhibition antamanide bioactive peptides UV-spectroscopy computational docking |
| title | Antamanide Analogs as Potential Inhibitors of Tyrosinase |
| title_full | Antamanide Analogs as Potential Inhibitors of Tyrosinase |
| title_fullStr | Antamanide Analogs as Potential Inhibitors of Tyrosinase |
| title_full_unstemmed | Antamanide Analogs as Potential Inhibitors of Tyrosinase |
| title_short | Antamanide Analogs as Potential Inhibitors of Tyrosinase |
| title_sort | antamanide analogs as potential inhibitors of tyrosinase |
| topic | tyrosinase inhibition antamanide bioactive peptides UV-spectroscopy computational docking |
| url | https://www.mdpi.com/1422-0067/23/11/6240 |
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