Log in

Relevant bibliographies by topics / Tyrosinase inhibitors / Journal articles

To see the other types of publications on this topic, follow the link: Tyrosinase inhibitors.

Journal articles on the topic 'Tyrosinase inhibitors'

Author: Grafiati

Published: 4 June 2021

Last updated: 20 February 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Tyrosinase inhibitors.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Kurihara, Hideyuki, and Kazuki Kujira. "Phlorotannins Derived From the Brown Alga Colpomenia bullosa as Tyrosinase Inhibitors." Natural Product Communications 16, no. 7 (2021): 1934578X2110213. http://dx.doi.org/10.1177/1934578x211021317.

Full text

Abstract:

Tyrosinase catalyzes hydroxylation of L-tyrosine and dehydrogenation of L-DOPA in the melanin biosynthesis pathway. Tyrosinase inhibitors have potential use as cosmetic whitening agents and for preventing seafood deterioration. In this report, tyrosinase inhibitors extracted from brown alga Colpomenia bullosa (Scytosiphonaceae, Scytosiphonales) were investigated. Inhibitory principles were isolated from the extract and identified as phlorotannins, phloroglucinol (1), diphlorethol (2), triphlorethol C (3), which have not been isolated in a free form previously, and fucophlorethol C (4). Compoun

APA, Harvard, Vancouver, ISO, and other styles

2

Li, Qi, Hongyu Yang, Jun Mo, et al. "Identification by shape-based virtual screening and evaluation of new tyrosinase inhibitors." PeerJ 6 (January 26, 2018): e4206. http://dx.doi.org/10.7717/peerj.4206.

Full text

Abstract:

Targeting tyrosinase is considered to be an effective way to control the production of melanin. Tyrosinase inhibitor is anticipated to provide new therapy to prevent skin pigmentation, melanoma and neurodegenerative diseases. Herein, we report our results in identifying new tyrosinase inhibitors. The shape-based virtual screening was performed to discover new tyrosinase inhibitors. Thirteen potential hits derived from virtual screening were tested by biological determinations. Compound 5186-0429 exhibited the most potent inhibitory activity. It dose-dependently inhibited the activity of tyrosi

APA, Harvard, Vancouver, ISO, and other styles

3

Kim, Chang, Sang Noh, Yujin Park та ін. "A Potent Tyrosinase Inhibitor, (E)-3-(2,4-Dihydroxyphenyl)-1-(thiophen-2-yl)prop-2-en-1-one, with Anti-Melanogenesis Properties in α-MSH and IBMX-Induced B16F10 Melanoma Cells". Molecules 23, № 10 (2018): 2725. http://dx.doi.org/10.3390/molecules23102725.

Full text

Abstract:

In this study, we designed and synthesized eight thiophene chalcone derivatives (1a–h) as tyrosinase inhibitors and evaluated their mushroom tyrosinase inhibitory activities. Of these eight compounds, (E)-3-(2,4-dihydroxyphenyl)-1-(thiophen-2-yl)prop-2-en-1-one (1c) showed strong competitive inhibition activity against mushroom tyrosinase with IC50 values of 0.013 μM for tyrosine hydroxylase and 0.93 μM for dopa oxidase. In addition, we used enzyme kinetics study and docking program to further evaluate the inhibitory mechanism of 1c toward tyrosinase. As an underlying mechanism of 1c mediated

APA, Harvard, Vancouver, ISO, and other styles

4

Choi, Joonhyeok, Trilok Neupane, Rishiram Baral, and Jun-Goo Jee. "Hydroxamic Acid as a Potent Metal-Binding Group for Inhibiting Tyrosinase." Antioxidants 11, no. 2 (2022): 280. http://dx.doi.org/10.3390/antiox11020280.

Full text

Abstract:

Tyrosinase, a metalloenzyme containing a dicopper cofactor, plays a central role in synthesizing melanin from tyrosine. Many studies have aimed to identify small-molecule inhibitors of tyrosinase for pharmaceutical, cosmetic, and agricultural purposes. In this study, we report that hydroxamic acid is a potent metal-binding group for interacting with dicopper atoms, thereby inhibiting tyrosinase. Hydroxamate-containing molecules, including anticancer drugs targeting histone deacetylase, vorinostat and panobinostat, significantly inhibited mushroom tyrosinase, with inhibitory constants in the su

APA, Harvard, Vancouver, ISO, and other styles

5

Micillo, Raffaella, Julia Sirés-Campos, José García-Borrón, Lucia Panzella, Alessandra Napolitano, and Conchi Olivares. "Conjugation with Dihydrolipoic Acid Imparts Caffeic Acid Ester Potent Inhibitory Effect on Dopa Oxidase Activity of Human Tyrosinase." International Journal of Molecular Sciences 19, no. 8 (2018): 2156. http://dx.doi.org/10.3390/ijms19082156.

Full text

Abstract:

Caffeic acid derivatives represent promising lead compounds in the search for tyrosinase inhibitors to be used in the treatment of skin local hyperpigmentation associated to an overproduction or accumulation of melanin. We recently reported the marked inhibitory activity of a conjugate of caffeic acid with dihydrolipoic acid, 2-S-lipoylcaffeic acid (LCA), on the tyrosine hydroxylase (TH) and dopa oxidase (DO) activities of mushroom tyrosinase. In the present study, we evaluated a more lipophilic derivative, 2-S-lipoyl caffeic acid methyl ester (LCAME), as an inhibitor of tyrosinase from human

APA, Harvard, Vancouver, ISO, and other styles

6

Honisch, Claudia, Matteo Gazziero, Roberto Dallocchio, et al. "Antamanide Analogs as Potential Inhibitors of Tyrosinase." International Journal of Molecular Sciences 23, no. 11 (2022): 6240. http://dx.doi.org/10.3390/ijms23116240.

Full text

Abstract:

The tyrosinase enzyme, which catalyzes the hydroxylation of monophenols and the oxidation of o-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 derivative

APA, Harvard, Vancouver, ISO, and other styles

7

Abuelizz, Hatem A., El Hassane Anouar, Mohamed Marzouk, et al. "Evaluation of Cytotoxic and Tyrosinase Inhibitory Activities of 2-phenoxy(thiomethyl) pyridotriazolopyrimidines: In Vitro and Molecular Docking Studies." Anti-Cancer Agents in Medicinal Chemistry 20, no. 14 (2020): 1714–21. http://dx.doi.org/10.2174/1871520620666200627212128.

Full text

Abstract:

Background: The use of tyrosinase has confirmed to be the best means of recognizing safe, effective, and potent tyrosinase inhibitors for whitening skin. Twenty-four 2-phenoxy(thiomethyl)pyridotriazolopyrimidines were synthesized and characterized in our previous studies. Objective: The present work aimed to evaluate their cytotoxicity against HepG2 (hepatocellular carcinoma), A549 (pulmonary adenocarcinoma), MCF-7 (breast adenocarcinoma) and WRL 68 (embryonic liver) cell lines. Methods: MTT assay was employed to investigate the cytotoxicity, and a tyrosinase inhibitor screening kit was used t

APA, Harvard, Vancouver, ISO, and other styles

8

Lee, Sanggwon, Heejeong Choi, Yujin Park, et al. "Urolithin and Reduced Urolithin Derivatives as Potent Inhibitors of Tyrosinase and Melanogenesis: Importance of the 4-Substituted Resorcinol Moiety." International Journal of Molecular Sciences 22, no. 11 (2021): 5616. http://dx.doi.org/10.3390/ijms22115616.

Full text

Abstract:

We previously reported (E)-β-phenyl-α,β-unsaturated carbonyl scaffold ((E)-PUSC) played an important role in showing high tyrosinase inhibitory activity and that derivatives with a 4-substituted resorcinol moiety as the β-phenyl group of the scaffold resulted in the greatest tyrosinase inhibitory activity. To examine whether the 4-substituted resorcinol moiety could impart tyrosinase inhibitory activity in the absence of the α,β-unsaturated carbonyl moiety of the (E)-PUSC scaffold, 10 urolithin derivatives were synthesized. To obtain more candidate samples, the lactone ring in synthesized urol

APA, Harvard, Vancouver, ISO, and other styles

9

Parveen, Naima, Sharique Akhtar Ali, and Ayesha Sharique Ali. "Insights Into the Explication of Potent Tyrosinase Inhibitors with Reference to Computational Studies." Letters in Drug Design & Discovery 16, no. 11 (2019): 1182–93. http://dx.doi.org/10.2174/1570180815666180803111021.

Full text

Abstract:

Background: Pigment melanin has primarily a photo defensive role in human skin, its unnecessary production and irregular distribution can cause uneven skin tone ultimately results in hyper pigmentation. Melanin biosynthesis is initiated by tyrosine oxidation through tyrosinase, the key enzyme for melanogenesis. Not only in humans, tyrosinase is also widely distributed in plants and liable for browning of vegetables and fruits. Search for the inhibitors of tyrosinase have been an important target to facilitate development of therapies for the prevention of hyperpigmentary disorders and an undes

APA, Harvard, Vancouver, ISO, and other styles

10

Pintus, Francesca, Delia Spanò, Angela Corona, and Rosaria Medda. "Antityrosinase activity ofEuphorbia characiasextracts." PeerJ 3 (October 13, 2015): e1305. http://dx.doi.org/10.7717/peerj.1305.

Full text

Abstract:

Tyrosinase is a well-known key enzyme in melanin biosynthesis and its inhibitors have become increasingly important because of their potential use as hypopigmenting agents. In the present study, the anti-melanogenic effect of aqueous and ethanolic extracts fromEuphorbia characiasleaves, stems, and flowers in cell-free and cellular systems was examined. All the extracts showed inhibitory effects against mushroom tyrosinase with leaf extracts exhibiting the lowest IC50values of 24 and 97 µg/mL for aqueous and ethanolic extracts respectively. Enzyme kinetic analysis indicated that leaf aqueous ex

APA, Harvard, Vancouver, ISO, and other styles

11

Choi, Heejeong, Il Young Ryu, Inkyu Choi, et al. "Novel Anti-Melanogenic Compounds, (Z)-5-(Substituted Benzylidene)-4-thioxothiazolidin-2-one Derivatives: In Vitro and In Silico Insights." Molecules 26, no. 16 (2021): 4963. http://dx.doi.org/10.3390/molecules26164963.

Full text

Abstract:

To confirm that the β-phenyl-α,β-unsaturated thiocarbonyl (PUSTC) scaffold, similar to the β-phenyl-α,β-unsaturated carbonyl (PUSC) scaffold, acts as a core inhibitory structure for tyrosinase, twelve (Z)-5-(substituted benzylidene)-4-thioxothiazolidin-2-one ((Z)-BTTZ) derivatives were designed and synthesized. Seven of the twelve derivatives showed stronger inhibitory activity than kojic acid against mushroom tyrosinase. Compound 2b (IC50 = 0.47 ± 0.97 µM) exerted a 141-fold higher inhibitory potency than kojic acid. Kinetic studies’ results confirmed that compounds 2b and 2f are competitive

APA, Harvard, Vancouver, ISO, and other styles

12

Matos, Maria João, Lourdes Santana, Eugenio Uriarte, et al. "Tyrosine-like condensed derivatives as tyrosinase inhibitors." Journal of Pharmacy and Pharmacology 64, no. 5 (2012): 742–46. http://dx.doi.org/10.1111/j.2042-7158.2012.01467.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Athipornchai, Anan, Nattisa Niyomtham, Wachirachai Pabuprapap, et al. "Potent Tyrosinase Inhibitory Activity of Curcuminoid Analogues and Inhibition Kinetics Studies." Cosmetics 8, no. 2 (2021): 35. http://dx.doi.org/10.3390/cosmetics8020035.

Full text

Abstract:

Natural tyrosinase inhibitors from herbal plants are promising therapeutic agents for skincare and cosmetic products. Natural curcuminoids exhibit weak antityrosinase properties. The structural modification of curcumin, the major curcuminoid from Curcuma longa, gave 14 analogues. The tyrosinase inhibitory activity of the natural curcuminoids and the modified analogues on both L-tyrosine and DOPA substrates were evaluated. The inhibition kinetics were also undertaken. For analogues with potent activity on the L-tyrosine substrate, the isoxazole analogue 12 and two reduced analogues, hexahydrocu

APA, Harvard, Vancouver, ISO, and other styles

14

Hwang, YeJi, Jieun Lee, Hee Jin Jung, et al. "A Novel Class of Potent Anti-Tyrosinase Compounds with Antioxidant Activity, 2-(Substituted phenyl)-5-(trifluoromethyl)benzo[d]thiazoles: In Vitro and In Silico Insights." Antioxidants 11, no. 7 (2022): 1375. http://dx.doi.org/10.3390/antiox11071375.

Full text

Abstract:

Sixteen compounds bearing a benzothiazole moiety were synthesized as potential tyrosinase inhibitors and evaluated for mushroom tyrosinase inhibitory activity. The compound 4-(5-(trifluoromethyl)benzo[d]thiazol-2-yl)benzene-1,3-diol (compound 1b) exhibited the highest tyrosinase activity inhibition, with an IC50 value of 0.2 ± 0.01 μM (a potency 55-fold greater than kojic acid). In silico results using mushroom tyrosinase and human tyrosinase showed that the 2,4-hydroxyl substituents on the phenyl ring of 1b played an important role in the inhibition of both tyrosinases. Kinetic studies on mus

APA, Harvard, Vancouver, ISO, and other styles

15

Huang, Yaru, Jiefang Yang, Yunyang Chi, et al. "Newly Designed Quinazolinone Derivatives as Novel Tyrosinase Inhibitor: Synthesis, Inhibitory Activity, and Mechanism." Molecules 27, no. 17 (2022): 5558. http://dx.doi.org/10.3390/molecules27175558.

Full text

Abstract:

We synthesized a series of quinazolinone derivates as tyrosinase inhibitors and evaluated their inhibition constants. We synthesized 2-(2,6-dimethylhepta-1,5-dien-1-yl)quinazolin-4(3H)-one (Q1) from the natural citral. The concentration, which led to 50% activity loss of Q1, was 103 ± 2 μM (IC50 = 103 ± 2 μM). Furthermore, we considered Q1 to be a mixed-type and reversible tyrosinase inhibitor, and determined the KI and KIS inhibition constants to be 117.07 μM and 423.63 μM, respectively. Our fluorescence experiment revealed that Q1 could interact with the substrates of tyrosine and L-DOPA in

APA, Harvard, Vancouver, ISO, and other styles

16

Yap, Pei-Gee, and Chee-Yuen Gan. "Multifunctional Tyrosinase Inhibitor Peptides with Copper Chelating, UV-Absorption and Antioxidant Activities: Kinetic and Docking Studies." Foods 10, no. 3 (2021): 675. http://dx.doi.org/10.3390/foods10030675.

Full text

Abstract:

Nature-derived tyrosinase inhibitors are of great industrial interest. Three monophenolase inhibitor peptides (MIPs) and three diphenolase inhibitor peptides (DIPs) from a previous study were investigated for their in vitro tyrosinase inhibitory effects, mode of inhibition, copper-chelating activity, sun protection factor (SPF) and antioxidant activities. DIP1 was found to be the most potent tyrosinase inhibitor (IC50 = 3.04 ± 0.39 mM), which could be due to the binding interactions between its aromatic amino acid residues (Y2 and D7) with tyrosinase hotspots (H85, V248, H258, H263, F264, R268

APA, Harvard, Vancouver, ISO, and other styles

17

Matos, Patrícia, António Paranhos, Maria Teresa Batista, and Artur Figueirinha. "Synergistic Effect of DIBOA and Verbascoside from Acanthus mollis Leaf on Tyrosinase Inhibition." International Journal of Molecular Sciences 23, no. 21 (2022): 13536. http://dx.doi.org/10.3390/ijms232113536.

Full text

Abstract:

Overexpression of melanin contributes to darkening of plant and fruit tissues and skin hyperpigmentation, leading to melasma or age spots. Although melanin biosynthesis is complex and involves several steps, a single enzyme known as tyrosinase is key to regulating this process. The melanogenesis pathway is initiated by oxidation of the starting material l-tyrosine (or l-DOPA) to dopaquinone by tyrosinase; the resulting quinone then serves as a substrate for subsequent steps that eventually lead to production of melanin. Medicinal plants are considered a good source of tyrosinase inhibitors. Th

APA, Harvard, Vancouver, ISO, and other styles

18

Iraji, Aida, Mahsima Khoshneviszadeh, Pegah Bakhshizadeh, Najmeh Edraki, and Mehdi Khoshneviszadeh. "Structure-Based Design, Synthesis, Biological Evaluation and Molecular Docking Study of 4-Hydroxy-N'-methylenebenzohydrazide Derivatives Acting as Tyrosinase Inhibitors with Potentiate Anti-Melanogenesis Activities." Medicinal Chemistry 16, no. 7 (2020): 892–902. http://dx.doi.org/10.2174/1573406415666190724142951.

Full text

Abstract:

Background: Melanogenesis is a process of melanin synthesis, which is a primary response for the pigmentation of human skin. Tyrosinase is a key enzyme, which catalyzes a ratelimiting step of the melanin formation. Natural products have shown potent inhibitors, but some of these possess toxicity. Numerous synthetic inhibitors have been developed in recent years may lead to the potent anti– tyrosinase agents. Objective: A number of 4-hydroxy-N'-methylenebenzohydrazide analogues with related structure to chalcone and tyrosine were constructed with various substituents at the benzyl ring of the m

APA, Harvard, Vancouver, ISO, and other styles

19

Hałdys, Katarzyna, Waldemar Goldeman, Natalia Anger-Góra, Joanna Rossowska, and Rafał Latajka. "Monosubstituted Acetophenone Thiosemicarbazones as Potent Inhibitors of Tyrosinase: Synthesis, Inhibitory Studies, and Molecular Docking." Pharmaceuticals 14, no. 1 (2021): 74. http://dx.doi.org/10.3390/ph14010074.

Full text

Abstract:

A set of 12 monosubstituted acetophenone thiosemicarbazone derivatives (TSCs) were synthesized and their inhibitory properties toward tyrosinase activity were tested. Moreover, their ability to inhibit melanogenesis in the B16F10 murine melanoma cell line was studied. In order to investigate the nature of interactions between the enzyme and the inhibitors, molecular docking to the active site was performed. TSCs 5, 6, 8, and 9 revealed a half maximal inhibitory concentration (IC50) below 1 µM. Compound 6 turned out to be the most potent tyrosinase inhibitor. All investigated compounds showed r

APA, Harvard, Vancouver, ISO, and other styles

20

Chaudhary, Dinesh, Fangchen Chong, Trilok Neupane, Joonhyeok Choi, and Jun-Goo Jee. "New Inhibitors of Laccase and Tyrosinase by Examination of Cross-Inhibition between Copper-Containing Enzymes." International Journal of Molecular Sciences 22, no. 24 (2021): 13661. http://dx.doi.org/10.3390/ijms222413661.

Full text

Abstract:

Coppers play crucial roles in the maintenance homeostasis in living species. Approximately 20 enzyme families of eukaryotes and prokaryotes are known to utilize copper atoms for catalytic activities. However, small-molecule inhibitors directly targeting catalytic centers are rare, except for those that act against tyrosinase and dopamine-β-hydroxylase (DBH). This study tested whether known tyrosinase inhibitors can inhibit the copper-containing enzymes, ceruloplasmin, DBH, and laccase. While most small molecules minimally reduced the activities of ceruloplasmin and DBH, aside from known inhibi

APA, Harvard, Vancouver, ISO, and other styles

21

Bonesi, Marco, Jianbo Xiao, Rosa Tundis, Francesca Aiello, Vincenzo Sicari, and Monica R. Loizzo. "Advances in the Tyrosinase Inhibitors from Plant Source." Current Medicinal Chemistry 26, no. 18 (2019): 3279–99. http://dx.doi.org/10.2174/0929867325666180522091311.

Full text

Abstract:

Tyrosinase is a multifunctional copper-containing oxidase which catalyses the oxidation of tyrosine to produce melanin. The alteration in melanin biosynthesis occurs in many diseases. The pigment has a protecting role against skin photo-carcinogenesis, but anomalous melanin pigmentation is an aesthetic problem in human beings. Moreover, the formation of neuromelanin in human brain could contribute to the neurodegeneration associated with Parkinson’s disease. Finally, tyrosinase is also responsible for undesired browning in fruits and vegetables. These topics encouraged the search for new inhib

APA, Harvard, Vancouver, ISO, and other styles

22

Pilevneli, Amine Dilara, and Belma Konuklugil. "Marine derived tyrosinase inhibitors." Ege Journal of Fisheries and Aquatic Sciences 37, no. 4 (2020): 427–36. http://dx.doi.org/10.12714/egejfas.37.4.15.

Full text

Abstract:

The cosmetics industry has gained strong momentum all over the world in recent years and has become a growing and promising sector. As it is known, as in the pharmaceutical industry, the cosmetic industry has also turned into becoming marine resources by seeking new materials for its continuation to be more productive for the field. To serve this purpose, marine-derived substances are highly claimed to be an interesting as well as a fruitful source for the benefits of the cosmetics industry. In this respect, as known globally, anti-tyrosinase inhibitors used in skin whitening are obtained from

APA, Harvard, Vancouver, ISO, and other styles

23

Kubo, Isao, and Ikuyo Kinst-Hori. "Tyrosinase Inhibitors from Cumin." Journal of Agricultural and Food Chemistry 46, no. 12 (1998): 5338–41. http://dx.doi.org/10.1021/jf980226+.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Misasa, Hirosuke, Yukiko Matsui, Hisao Uehara, Hiroshi Tanaka, Miki Ishihara, and Hisao Shibata. "Tyrosinase Inhibitors fromAlbatrellus confluens." Bioscience, Biotechnology, and Biochemistry 56, no. 10 (1992): 1660–61. http://dx.doi.org/10.1271/bbb.56.1660.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Yin, Xing-shuo, Xue-qin Zhang, Jin-tuo Yin, De-zhi Kong, and De-qiang Li. "Screening and identification of potential tyrosinase inhibitors from Semen Oroxyli extract by ultrafiltration LC-MS and in silico molecular docking." Journal of Chromatographic Science 57, no. 9 (2019): 838–46. http://dx.doi.org/10.1093/chromsci/bmz054.

Full text

Abstract:

Abstract There is an increasing interest in screening and developing natural tyrosinase inhibitors widely applied in medicinal and cosmetic products, as well as in the food industry. In this study, an approach by ultrafiltration LC-MS and molecular docking was used to screen and identify tyrosinase inhibitors from Semen Oroxyli extract. The samples were first incubated with the tyrosinase to select the optimal binding conditions including tyrosinase concentration, incubation time and the molecular weight of ultrafiltration membrane. By comparison of the chromatographic profiles of the extracts

APA, Harvard, Vancouver, ISO, and other styles

26

Yamazaki, Yoshimitsu, and Yasuhiro Kawano. "Inhibitory Effect of Hydroxyindoles and their Analogues on Human Melanoma Tyrosinase." Zeitschrift für Naturforschung C 65, no. 1-2 (2010): 49–54. http://dx.doi.org/10.1515/znc-2010-1-209.

Full text

Abstract:

A recent study showed that N-acylserotonin derivatives have strong inhibitory activity against tyrosinase. To clarify the role of the 5-hydroxy group in the indole ring, 2-, 4-, 5-, 6-, and 7-hydroxyindole and 11 related compounds such as 5-hydroxyindan and 6-hydroxyquinoline were tested for their inhibition of catecholase activity of tyrosinase from human HMVII melanoma cells. 6-Hydroxyindole (5) and 7-hydroxyindole (6) were potent inhibitors, while 5-hydroxyindole (4) was a weaker inhibitor than the above-mentioned compounds (IC50 = 20, 79, 366, and 342 μM for 5, 6, 4, and kojic acid, respec

APA, Harvard, Vancouver, ISO, and other styles

27

Nazir, Yasir, Hummera Rafique, Naghmana Kausar, et al. "Methoxy-Substituted Tyramine Derivatives Synthesis, Computational Studies and Tyrosinase Inhibitory Kinetics." Molecules 26, no. 9 (2021): 2477. http://dx.doi.org/10.3390/molecules26092477.

Full text

Abstract:

Targeting tyrosinase for melanogenesis disorders is an established strategy. Hydroxyl-substituted benzoic and cinnamic acid scaffolds were incorporated into new chemotypes that displayed in vitro inhibitory effects against mushroom and human tyrosinase for the purpose of identifying anti-melanogenic ingredients. The most active compound 2-((4-methoxyphenethyl)amino)-2-oxoethyl (E)-3-(2,4-dihydroxyphenyl) acrylate (Ph9), inhibited mushroom tyrosinase with an IC50 of 0.059 nM, while 2-((4-methoxyphenethyl)amino)-2-oxoethyl cinnamate (Ph6) had an IC50 of 2.1 nM compared to the positive control, k

APA, Harvard, Vancouver, ISO, and other styles

28

Manandhar, Wagle, Seong, et al. "Phlorotannins with Potential Anti-tyrosinase and Antioxidant Activity Isolated from the Marine Seaweed Ecklonia stolonifera." Antioxidants 8, no. 8 (2019): 240. http://dx.doi.org/10.3390/antiox8080240.

Full text

Abstract:

Compounds were isolated from Ecklonia stolonifera Okamura, a marine brown alga widely consumed as food. Among the isolated compounds, 974-A was demonstrated for the first time to be a potent competitive inhibitor of mushroom tyrosinase activity towards l-tyrosine and l-DOPA (IC50 values = 1.57 ± 0.08 and 3.56 ± 0.22 µM, respectively). Molecular docking simulations clarified that the hydroxyl residues of the isolated compounds formed hydrogen bonds with residues at the catalytic and allosteric sites of tyrosinase, while other residues participated in hydrophobic interactions. Moreover, 974-A, p

APA, Harvard, Vancouver, ISO, and other styles

29

Politi, Maria Evgenia, Kostas Bethanis, Trias Thireou, and Elias Christoforides. "Glycosidic vs. Aglycol Form of Natural Products as Putative Tyrosinase Inhibitors." Biophysica 1, no. 4 (2021): 458–73. http://dx.doi.org/10.3390/biophysica1040033.

Full text

Abstract:

Numerous natural products and designed molecules have been evaluated as tyrosinase inhibitors that impede enzymes’ oxidation activity. In the present study, new potent natural inhibitors were retrieved from the ZINC database by the similarity-screening of 37 previously reported tyrosinase inhibitors. The screening resulted in 42 candidate inhibitory molecules that were categorized into five groups. Molecular-docking analysis for these compounds, as well as for three others known for their inhibition activity (caffeic acid, naringenin, and gallic acid), was carried out against the tyrosinase st

APA, Harvard, Vancouver, ISO, and other styles

30

Paudel, Pradeep, Aditi Wagle, Su Hui Seong, Hye Jin Park, Hyun Ah Jung, and Jae Sue Choi. "A New Tyrosinase Inhibitor from the Red Alga Symphyocladia latiuscula (Harvey) Yamada (Rhodomelaceae)." Marine Drugs 17, no. 5 (2019): 295. http://dx.doi.org/10.3390/md17050295.

Full text

Abstract:

A marine red alga, Symphyocladia latiuscula (Harvey) Yamada (Rhodomelaceae), is a rich source of bromophenols with a wide array of biological activities. This study investigates the anti-tyrosinase activity of the alga. Moderate activity was demonstrated by the methanol extract of S. latiuscula, and subsequent column chromatography identified three bromophenols: 2,3,6-tribromo-4,5-dihydroxybenzyl methyl alcohol (1), 2,3,6-tribromo-4,5-dihydroxybenzyl methyl ether (2), and bis-(2,3,6-tribromo-4,5-dihydroxybenzyl methyl ether) (3). Bromophenols 1 and 3 exhibited potent competitive tyrosinase inh

APA, Harvard, Vancouver, ISO, and other styles

31

Durai, Prasannavenkatesh, Young-Joon Ko, Jin-Chul Kim, Cheol-Ho Pan, and Keunwan Park. "Identification of Tyrosinase Inhibitors and Their Structure-Activity Relationships via Evolutionary Chemical Binding Similarity and Structure-Based Methods." Molecules 26, no. 3 (2021): 566. http://dx.doi.org/10.3390/molecules26030566.

Full text

Abstract:

Tyrosinase is an enzyme that plays a crucial role in the melanogenesis of humans and the browning of food products. Thus, tyrosinase inhibitors that are useful to the cosmetic and food industries are required. In this study, we have used evolutionary chemical binding similarity (ECBS) to screen a virtual chemical database for human tyrosinase, which resulted in seven potential tyrosinase inhibitors confirmed through the tyrosinase inhibition assay. The tyrosinase inhibition percentage for three of the new actives was over 90% compared to 61.9% of kojic acid. From the structural analysis throug

APA, Harvard, Vancouver, ISO, and other styles

32

Widelski, Jarosław, Katarzyna Gaweł-Bęben, Karolina Czech, et al. "Extracts from European Propolises as Potent Tyrosinase Inhibitors." Molecules 28, no. 1 (2022): 55. http://dx.doi.org/10.3390/molecules28010055.

Full text

Abstract:

Tyrosinase is a key enzyme in the melanogenesis pathway. Melanin, the product of this process, is the main pigment of the human skin and a major protection factor against harmful ultraviolet radiation (UVR). Increased melanin synthesis due to tyrosinase hyperactivity can cause hyperpigmentation disorders, which in consequence causes freckles, age spots, melasma, or postinflammatory hyperpigmentation. Tyrosinase overproduction and hyperactivity are triggered by the ageing processes and skin inflammation as a result of oxidative stress. Therefore, the control of tyrosinase activity is the main g

APA, Harvard, Vancouver, ISO, and other styles

33

Liu, Haichun, Yitian Zhu, Ting Wang, Jin Qi, and Xuming Liu. "Enzyme-Site Blocking Combined with Optimization of Molecular Docking for Efficient Discovery of Potential Tyrosinase Specific Inhibitors from Puerariae lobatae Radix." Molecules 23, no. 10 (2018): 2612. http://dx.doi.org/10.3390/molecules23102612.

Full text

Abstract:

Enzyme inhibitors from natural products are becoming an attractive target for drug discovery and development; however, separating enzyme inhibitors from natural-product extracts is highly complex. In this study, we developed a strategy based on tyrosinase-site blocking ultrafiltration integrated with HPLC-QTOF-MS/MS and optimized molecular docking to screen tyrosinase inhibitors from Puerariae lobatae Radix extract. Under optimized ultrafiltration parameters, we previously used kojic acid, a known tyrosinase inhibitor, to block the tyrosinase active site in order to eliminate false-positive re

APA, Harvard, Vancouver, ISO, and other styles

34

Sabrina Benouis, Sabrina Benouis, Fouad Ferkous Fouad Ferkous, Khairedine Kraim Khairedine Kraim, Ahmed Allali Ahmed Allali, and Youcef Saihi Youcef Saihi. "Molecular Docking Studies on Gingerol Analogues toward Mushroom Tyrosinase." Journal of the chemical society of pakistan 42, no. 2 (2020): 214. http://dx.doi.org/10.52568/000630.

Full text

Abstract:

The gingerol presents the starting point of our work which aims to discover new inhibitors of the tyrosinase enzyme. Therefore, we have studied the activity of gingerol derivatives as inhibitors against mushroom tyrosinase based on the molecular docking. Molecular docking studies were performed on a series of gingerol analogues retrieved from Zinc database (with 70% as similarity threshold). The gingerol analogues were docked within the active site region of mushroom tyrosinase (PDB: 2Y9X) using Molegro Virtual Docker V.5.0. The results of molecular docking studies revealed that some analogues

APA, Harvard, Vancouver, ISO, and other styles

35

Sabrina Benouis, Sabrina Benouis, Fouad Ferkous Fouad Ferkous, Khairedine Kraim Khairedine Kraim, Ahmed Allali Ahmed Allali, and Youcef Saihi Youcef Saihi. "Molecular Docking Studies on Gingerol Analogues toward Mushroom Tyrosinase." Journal of the chemical society of pakistan 42, no. 2 (2020): 214. http://dx.doi.org/10.52568/000630/jcsp/42.02.2020.

Full text

Abstract:

The gingerol presents the starting point of our work which aims to discover new inhibitors of the tyrosinase enzyme. Therefore, we have studied the activity of gingerol derivatives as inhibitors against mushroom tyrosinase based on the molecular docking. Molecular docking studies were performed on a series of gingerol analogues retrieved from Zinc database (with 70% as similarity threshold). The gingerol analogues were docked within the active site region of mushroom tyrosinase (PDB: 2Y9X) using Molegro Virtual Docker V.5.0. The results of molecular docking studies revealed that some analogues

APA, Harvard, Vancouver, ISO, and other styles

36

Yang, Seo Young, Jang Hoon Kim, Xiangdong Su, and Jeong Ah Kim. "The Luteolinidin and Petunidin 3-O-Glucoside: A Competitive Inhibitor of Tyrosinase." Molecules 27, no. 17 (2022): 5703. http://dx.doi.org/10.3390/molecules27175703.

Full text

Abstract:

The enzyme tyrosinase plays a key role in the early stages of melanin biosynthesis. This study evaluated the inhibitory activity of anthocyanidin (1) and anthocyanins (2–6) on the catalytic reaction. Of the six derivatives examined, 1–3 showed inhibitory activity with IC50 values of 3.7 ± 0.1, 10.3 ± 1.0, and 41.3 ± 3.2 μM, respectively. Based on enzyme kinetics, 1–3 were confirmed to be competitive inhibitors with Ki values of 2.8, 9.0, and 51.9 μM, respectively. Molecular docking analysis revealed the formation of a binary encounter complex between 1–3 and the tyrosinase catalytic site. Lute

APA, Harvard, Vancouver, ISO, and other styles

37

Lee, Jieun, Yu Jung Park, Hee Jin Jung, et al. "Design and Synthesis of (Z)-2-(Benzylamino)-5-benzylidenethiazol-4(5H)-one Derivatives as Tyrosinase Inhibitors and Their Anti-Melanogenic and Antioxidant Effects." Molecules 28, no. 2 (2023): 848. http://dx.doi.org/10.3390/molecules28020848.

Full text

Abstract:

In this study, (Z)-2-(benzylamino)-5-benzylidenethiazol-4(5H)-one (BABT) derivatives were designed as tyrosinase inhibitors based on the structure of MHY2081, using a simplified approach. Of the 14 BABT derivatives synthesized, two derivatives ((Z)-2-(benzylamino)-5-(3-hydroxy-4-methoxybenzylidene)thiazol-4(5H)-one [7] and (Z)-2-(benzylamino)-5-(2,4-dihydroxybenzylidene)thiazol-4(5H)-one [8]) showed more potent mushroom tyrosinase inhibitory activities than kojic acid, regardless of the substrate used; in particular, compound 8 was 106-fold more potent than kojic acid when l-tyrosine was used

APA, Harvard, Vancouver, ISO, and other styles

38

Caixeiro, Janaína M. R., Vinicius T. Gonçalves, Márcia C. C. de Oliveira, Carlos M. R. Sant'Anna, Victor M. Rumjanek, and João B. N. DaCosta. "Dialkylphosphorylhydrazones as potent tyrosinase inhibitors." Journal of the Brazilian Chemical Society 23, no. 5 (2012): 804–9. http://dx.doi.org/10.1590/s0103-50532012000500003.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Likhitwitayawuid, Kittisak, Boonchoo Sritularak, and Wanchai De-Eknamkul. "Tyrosinase Inhibitors from Artocarpus gomezianus." Planta Medica 66, no. 03 (2000): 275–77. http://dx.doi.org/10.1055/s-2000-8656.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

SHIROTA, Sachiko, Kouji MIYAZAKI, Ritsuo AIYAMA, Minoru ICHIOKA, and Teruo YOKOKURA. "Tyrosinase Inhibitors from Crude Drugs." Biological & Pharmaceutical Bulletin 17, no. 2 (1994): 266–69. http://dx.doi.org/10.1248/bpb.17.266.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Kubo, Isao, and Ikuyo Kinst-Hori. "Tyrosinase Inhibitors from Anise Oil." Journal of Agricultural and Food Chemistry 46, no. 4 (1998): 1268–71. http://dx.doi.org/10.1021/jf9708958.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Khotimchenko, Y. S. "Tyrosinase inhibitors from marine algae." British Journal of Dermatology 175, no. 3 (2016): 457–58. http://dx.doi.org/10.1111/bjd.14730.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Lee, Nan Kyoung, Kun Ho Son, Hyeun Wook Chang, et al. "Prenylated flavonoids as tyrosinase inhibitors." Archives of Pharmacal Research 27, no. 11 (2004): 1132–35. http://dx.doi.org/10.1007/bf02975118.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Şabudak, Temine, Mahmut Tareq Hassan Khan, M. Iqbal Choudhary, and Sevil Oksuz. "Potent tyrosinase inhibitors fromTrifolium balansae." Natural Product Research 20, no. 7 (2006): 665–70. http://dx.doi.org/10.1080/14786410500196821.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Wei, Lan-Yi, Wei Lin, Bey-Fen Leo, Lik-Voon Kiew, Chia-Ching Chang, and Chiun-Jye Yuan. "Development of the Sensing Platform for Protein Tyrosine Kinase Activity." Biosensors 11, no. 7 (2021): 240. http://dx.doi.org/10.3390/bios11070240.

Full text

Abstract:

A miniature tyrosinase-based electrochemical sensing platform for label-free detection of protein tyrosine kinase activity was developed in this study. The developed miniature sensing platform can detect the substrate peptides for tyrosine kinases, such as c-Src, Hck and Her2, in a low sample volume (1–2 μL). The developed sensing platform exhibited a high reproducibility for repetitive measurement with an RSD (relative standard deviation) of 6.6%. The developed sensing platform can detect the Hck and Her2 in a linear range of 1–200 U/mL with the detection limit of 1 U/mL. The sensing platform

APA, Harvard, Vancouver, ISO, and other styles

46

Jung, Sang Won, Kyeong Lee, and Art E. Cho. "Computational approaches to predict binding interactions between mammalian tyrosinases and (S)-(+)-decursin and its analogues as potent inhibitors." RSC Advances 6, no. 52 (2016): 46765–74. http://dx.doi.org/10.1039/c6ra09365e.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Kim, Jang Hoon, Sunggun Lee, Saerom Park, Ji Soo Park, Young Ho Kim, and Seo Young Yang. "Slow-Binding Inhibition of Tyrosinase by Ecklonia cava Phlorotannins." Marine Drugs 17, no. 6 (2019): 359. http://dx.doi.org/10.3390/md17060359.

Full text

Abstract:

Tyrosinase inhibitors improve skin whitening by inhibiting the formation of melanin precursors in the skin. The inhibitory activity of seven phlorotannins (1–7), triphlorethol A (1), eckol (2), 2-phloroeckol (3), phlorofucofuroeckol A (4), 2-O-(2,4,6-trihydroxyphenyl)-6,6′-bieckol (5), 6,8′-bieckol (6), and 8,8′-bieckol (7), from Ecklonia cava was tested against tyrosinase, which converts tyrosine into dihydroxyphenylalanine. Compounds 3 and 5 had IC50 values of 7.0 ± 0.2 and 8.8 ± 0.1 μM, respectively, in competitive mode, with Ki values of 8.2 ± 1.1 and 5.8 ± 0.8 μM. Both compounds showed th

APA, Harvard, Vancouver, ISO, and other styles

48

Nazir, Yasir, Hummera Rafique, Sadia Roshan, et al. "Molecular Docking, Synthesis, and Tyrosinase Inhibition Activity of Acetophenone Amide: Potential Inhibitor of Melanogenesis." BioMed Research International 2022 (January 11, 2022): 1–10. http://dx.doi.org/10.1155/2022/1040693.

Full text

Abstract:

Tyrosinase and its related proteins are responsible for pigmentation disorders, and inhibiting tyrosinase is an established strategy to treat hyperpigmentation. The carbonyl scaffolds can be effective inhibitors of tyrosinase activity, and the fact that both benzoic and cinnamic acids are safe natural substances with such a scaffolded structure, it was speculated that hydroxyl-substituted benzoic and cinnamic acid derivatives may exhibit potent tyrosinase inhibitory activity. These moieties were incorporated into new chemotypes that displayed in vitro inhibitory effect against mushroom tyrosin

APA, Harvard, Vancouver, ISO, and other styles

49

Hashim, Farah J., Sukanda Vichitphan, Jaehong Han, and Kanit Vichitphan. "Alternative Approach for Specific Tyrosinase Inhibitor Screening: Uncompetitive Inhibition of Tyrosinase by Moringa oleifera." Molecules 26, no. 15 (2021): 4576. http://dx.doi.org/10.3390/molecules26154576.

Full text

Abstract:

Tyrosinase (TYR) is a type III copper oxidase present in fungi, plants and animals. The inhibitor of human TYR plays a vital role in pharmaceutical and cosmetic fields by preventing synthesis of melanin in the skin. To search for an effective TYR inhibitor from various plant extracts, a kinetic study of TYR inhibition was performed with mushroom TYR. Among Panax ginseng, Alpinia galanga, Vitis vinifera and Moringa oleifera, the extracts of V. vinifera seed, A. galanga rhizome and M. oleifera leaf reversibly inhibited TYR diphenolase activity with IC50 values of 94.8 ± 0.2 µg/mL, 105.4 ± 0.2 µg

APA, Harvard, Vancouver, ISO, and other styles

50

Lin, Yung-Sheng, Hui-Ju Chen, Jung-Ping Huang, et al. "Kinetics of Tyrosinase Inhibitory Activity Using Vitis vinifera Leaf Extracts." BioMed Research International 2017 (2017): 1–5. http://dx.doi.org/10.1155/2017/5232680.

Full text

Abstract:

Natural medical plant is considered as a good source of tyrosinase inhibitors. Red vine leaf extract (RVLE) can be applied to a wide variety of medical disciplines, such as treatments for chronic venous insufficiency over many decades. This study investigated the tyrosinase inhibitory activity of RVLE containing gallic acid, chlorogenic acid, epicatechin, rutin, and resveratrol which are effective for skin hyperpigmentation. The five components contents are 1.03, 0.2, 18.55, 6.45, and 0.48 mg/g for gallic acid, chlorogenic acid, epicatechin, rutin, and resveratrol. The kinetic study showed the

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!