Login Register Cart 0
Generic placeholder image

Current Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 0929-8673
ISSN (Online): 1875-533X

Back
Journal Home About Journal Editorial Board Journal Insight Current Issue Volumes/Issues
Subscribe
Review Article

Novel Synthesized Tyrosinase Inhibitors: A Systematic Patent Review (2012-Present)

Author(s): Erika Beltran, Mairim Russo Serafini, Izabel Almeida Alves and Diana Marcela Aragón Novoa*

Volume 31, Issue 3, 2024

Published on: 21 March, 2023

Page: [308 - 335] Pages: 28

DOI: 10.2174/0929867330666230203111437

Price: $65

Abstract

Tyrosine is an enzyme responsible for melanin production. Its abnormal accumulation in different parts of the body is known as hyperpigmentation. Tyrosinase inhibitors have been used as one of the main approaches to treat these kinds of cosmetic and medical issues. This review aimed to discuss the advances in patents for this class of inhibitors, focusing on synthetic ones, by studying recent patent applications (2012-2022). We performed a screening using the European Patent Office’s Espacenet database, from which 15 inventions were selected and fully studied. China has more patent applications, all of them were focused on synthetic methods and the majority declared at least two additional applications as antibrowning agents for fruits and vegetables, biological pesticides, and medicine to treat diseases like Parkinson’s or melanoma. The strategies employed by the investigators focused on the examination of previous literature, which oriented on the type of structures that have been found to show good inhibitory activity; the study also examined aspects of their reaction mechanisms and information about the structureactivity relationship. For some groups of inhibitors, such as benzaldehyde and anthraquinone derivatives, the data were meaningful and extensive. In contrast, arginyl and troponoids compounds were difficult to analyze due to the limited research works.

« Previous Next »
[1]
Kim, Y.J.; Uyama, H. Tyrosinase inhibitors from natural and synthetic sources: Structure, inhibition mechanism and perspective for the future. Cell. Mol. Life Sci., 2005, 62(15), 1707-1723.
[http://dx.doi.org/10.1007/s00018-005-5054-y] [PMID: 15968468]
[2]
Chang, T.S. An updated review of tyrosinase inhibitors. Int. J. Mol. Sci., 2009, 10(6), 2440-2475.
[http://dx.doi.org/10.3390/ijms10062440] [PMID: 19582213]
[3]
Schallreuter, K.U.; Kothari, S.; Chavan, B.; Spencer, J.D. Regulation of melanogenesis - controversies and new concepts. Exp. Dermatol., 2008, 17(5), 395-404.
[http://dx.doi.org/10.1111/j.1600-0625.2007.00675.x] [PMID: 18177348]
[4]
Sánchez-Ferrer, Á.; Rodríguez-López, N.J.; García-Cánovas, F.; García-Carmona, F. Tyrosinase: A comprehensive review of its mechanism. Biochim. Biophys. Acta Protein Struct. Mol. Enzymol., 1995, 1247(1), 1-11.
[http://dx.doi.org/10.1016/0167-4838(94)00204-T]
[5]
Zeng, H.; Sun, D.; Chu, S.; Zhang, J.; Hu, G.; Yang, R. Inhibitory effects of four anthraquinones on tyrosinase activity: Insight from spectroscopic analysis and molecular docking. Int. J. Biol. Macromol., 2020, 160, 153-163.
[http://dx.doi.org/10.1016/j.ijbiomac.2020.05.193] [PMID: 32464200]
[6]
Knight, H. Patent strategy for researchers and research managers, (3rd ed.); Willy: New Jersey, USA, 2013.
[7]
Peters, P. Mind the gap: Spanning the divide between patents and journal articles. 2019. Available from: https://www.cas.org/resources/blog/mind-gap-spanning-divide-between-patents-and-journal-articles [accessed Aug 12, 2022].
[8]
Chen, C.; Lin, L.; Yang, W.; Bordon, J.; Wang, D.H. An updated organic classification of tyrosinase inhibitors on melanin biosynthesis. Curr. Org. Chem., 2015, 19(1), 4-18.
[http://dx.doi.org/10.2174/1385272819666141107224806]
[9]
Chen, L.H.; Hu, Y.H.; Song, W.; Song, K.K.; Liu, X.; Jia, Y.L.; Zhuang, J.X.; Chen, Q.X. Synthesis and antityrosinase mechanism of benzaldehyde thiosemicarbazones: Novel tyrosinase inhibitors. J. Agric. Food Chem., 2012, 60(6), 1542-1547.
[http://dx.doi.org/10.1021/jf204420x] [PMID: 22250887]
[10]
Lee, S.Y.; Baek, N.; Nam, T. Natural, semisynthetic and synthetic tyrosinase inhibitors. J. Enzyme Inhib. Med. Chem., 2016, 31(1), 1-13.
[http://dx.doi.org/10.3109/14756366.2015.1004058] [PMID: 25683082]
[11]
Kubo, I.; Chen, Q.X.; Nihei, K. Molecular design of antibrowning agents: antioxidative tyrosinase inhibitors. Food Chem., 2003, 81(2), 241-247.
[http://dx.doi.org/10.1016/S0308-8146(02)00418-1]
[12]
Yi, W.; Wu, X.; Cao, R.; Song, H.; Ma, L. Biological evaluations of novel vitamin C esters as mushroom tyrosinase inhibitors and antioxidants. Food Chem., 2009, 117(3), 381-386.
[http://dx.doi.org/10.1016/j.foodchem.2009.03.108]
[13]
Ullah, S.; Son, S.; Yun, H.; Kim, D.; Chun, P.; Moon, H. Tyrosinase inhibitors: A patent review (2011-2015). Expert Opin. Ther. Pat., 2016, 26(3), 347-362.
[http://dx.doi.org/10.1517/13543776.2016.1146253] [PMID: 26815044]
[14]
Peng, Z.; Wang, G.; Zeng, Q.H.; Li, Y.; Liu, H.; Wang, J.J.; Zhao, Y. A systematic review of synthetic tyrosinase inhibitors and their structure-activity relationship. Crit. Rev. Food Sci. Nutr., 2022, 62(15), 4053-4094.
[http://dx.doi.org/10.1080/10408398.2021.1871724] [PMID: 33459057]
[15]
Tokudome, Y.; Hoshi, T.; Mori, S.; Hijikuro, I. Synthesis of resorcinol derivatives and their effects on melanin production. Cosmetics, 2020, 7(3), 55.
[http://dx.doi.org/10.3390/cosmetics7030055]
[16]
Khatib, S.; Nerya, O.; Musa, R.; Tamir, S.; Peter, T.; Vaya, J. Enhanced substituted resorcinol hydrophobicity augments tyrosinase inhibition potency. J. Med. Chem., 2007, 50(11), 2676-2681.
[http://dx.doi.org/10.1021/jm061361d] [PMID: 17447749]
[17]
Shimizu, K.; Kondo, R.; Sakai, K.; Takeda, N.; Nagahata, T.; Oniki, T. Novel vitamin E derivative with 4-substituted resorcinol moiety has both antioxidant and tyrosinase inhibitory properties. Lipids, 2001, 36(12), 1321-1326.
[http://dx.doi.org/10.1007/s11745-001-0847-9] [PMID: 11834083]
[18]
Ha, K.S.; Jo, S.H.; Kang, B.H.; Apostolidis, E.; Lee, M.S.; Jang, H.D.; Kwon, Y.I. In vitro and in vivo antihyperglycemic effect of 2 amadori rearrangement compounds, arginyl-fructose and arginyl-fructosyl-glucose. J. Food Sci., 2011, 76(8), H188-H193.
[http://dx.doi.org/10.1111/j.1750-3841.2011.02361.x] [PMID: 22417590]
[19]
Zhao, J.; Zhao, J. Plant troponoids: Chemistry, biological activity, and biosynthesis. Curr. Med. Chem., 2007, 14(24), 2597-2621.
[http://dx.doi.org/10.2174/092986707782023253] [PMID: 17979713]
[20]
Pereira, D.M.; Valentão, P.; Andrade, P.B. Marine natural pigments: Chemistry, distribution and analysis. Dyes Pigments, 2014, 111, 124-134.
[http://dx.doi.org/10.1016/j.dyepig.2014.06.011]
[21]
Phutim-Mangkhalthon, A.; Teerakapong, A.; Tippayawat, P.; Morales, N.P.; Morkmued, S.; Puasiri, S.; Priprem, A.; Damrongrungruang, T. Anti-inflammatory effect of photodynamic therapy using guaiazulene and red lasers on peripheral blood mononuclear cells. Photodiagn. Photodyn. Ther., 2020, 31, 101747.
[http://dx.doi.org/10.1016/j.pdpdt.2020.101747] [PMID: 32200021]
[22]
Zolghadri, S.; Bahrami, A.; Hassan Khan, M.T.; Munoz-Munoz, J.; Garcia-Molina, F.; Garcia-Canovas, F.; Saboury, A.A. A comprehensive review on tyrosinase inhibitors. J. Enzyme Inhib. Med. Chem., 2019, 34(1), 279-309.
[http://dx.doi.org/10.1080/14756366.2018.1545767] [PMID: 30734608]
[23]
Yaari, Z.; Cheung, J.M.; Baker, H.A.; Frederiksen, R.S.; Jena, P.V.; Horoszko, C.P.; Jiao, F.; Scheuring, S.; Luo, M.; Heller, D.A. Nanoreporter of an enzymatic suicide inactivation pathway. Nano Lett., 2020, 20(11), 7819-7827.
[http://dx.doi.org/10.1021/acs.nanolett.0c01858] [PMID: 33119310]
[24]
Obaid, R.J.; Mughal, E.U.; Naeem, N.; Sadiq, A.; Alsantali, R.I.; Jassas, R.S.; Moussa, Z.; Ahmed, S.A. Natural and synthetic flavonoid derivatives as new potential tyrosinase inhibitors: A systematic review. RSC Advances, 2021, 11(36), 22159-22198.
[http://dx.doi.org/10.1039/D1RA03196A] [PMID: 35480807]
[25]
Tseng, T.S.; Tsai, K.C.; Chen, W.C.; Wang, Y.T.; Lee, Y.C.; Lu, C.K.; Don, M.J.; Chang, C.Y.; Lee, C.H.; Lin, H.H.; Hsu, H.J.; Hsiao, N.W. Discovery of potent cysteine-containing dipeptide inhibitors against tyrosinase: A comprehensive investigation of 20 × 20 dipeptides in inhibiting dopachrome formation. J. Agric. Food Chem., 2015, 63(27), 6181-6188.
[http://dx.doi.org/10.1021/acs.jafc.5b01026] [PMID: 26083974]
[26]
García-Molina, F.; Muñoz, J.L.; Varón, R.; Rodríguez-López, J.N.; García-Cánovas, F.; Tudela, J. A review on spectrophotometric methods for measuring the monophenolase and diphenolase activities of tyrosinase. J. Agric. Food Chem., 2007, 55(24), 9739-9749.
[http://dx.doi.org/10.1021/jf0712301] [PMID: 17958393]
[27]
Bassiri, E. Molecular biology of life laboratory, Available from: https://www.sas.upenn.edu/labmanuals/biol123/Table _of_Contents_files/8b-EnzymeKinetics-Spec.pdf [accessed Aug 12, 2022].
[28]
Raynie, D. The vital role of blanks in sample preparation. LC GC N. Am., 2018, 36(8), 494-497.
[29]
Mukherjee, P. Quality control and evaluation of herbal drugs. Evaluating Natural Products and Traditional Medicine, (1st Ed.); Elsevier: Amsterdam, 2019, pp. 515-537.
[http://dx.doi.org/10.1016/B978-0-12-813374-3.00013-2]
[30]
Caldwell, G.W.; Yan, Z.; Lang, W.; Masucci, J.A. The IC(50) concept revisited. Curr. Top. Med. Chem., 2012, 12(11), 1282-1290.
[http://dx.doi.org/10.2174/156802612800672844] [PMID: 22571790]

Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy