共查询到20条相似文献,搜索用时 31 毫秒
1.
Effect of Kojic Acid on the Oxidation of DL-DOPA,Norepinephrine, and Dopamine by Mushroom Tyrosinase
VARDA KAHN 《Pigment cell & melanoma research》1995,8(5):234-240
Kojic acid inhibits effectively the rate of formation of pigmented product(s) and of oxygen uptake when DL-DOPA, norepinephrine and dopamine are oxidized by mushroom tyrosinase. In addition to the direct effect of kojic acid on the enzyme, kojic acid also affects the UV-VIS spectrum of the final product(s) formed, this being due to the ability of the o-quinones of these substrates to oxidize kojic acid to a yellow product(s). Kojic acid can thus prevent the conversion of the o-quinones of DL-DOPA, norepinephrine and dopamine to their corresponding melanin. 相似文献
2.
Antioxidant,anti-tyrosinase and anti-melanogenic effects of (E)-2,3-diphenylacrylic acid derivatives
《Bioorganic & medicinal chemistry》2019,27(11):2192-2200
During our continued search for strong skin whitening agents over the past ten years, we have investigated the efficacies of many tyrosinase inhibitors containing a common (E)-β-phenyl-α,β-unsaturated carbonyl scaffold, which we found to be essential for the effective inhibition of mushroom and mammalian tyrosinases. In this study, we explored the tyrosinase inhibitory effects of 2,3-diphenylacrylic acid (2,3-DPA) derivatives, which also possess the (E)-β-phenyl-α,β-unsaturated carbonyl motif. We synthesized fourteen (E)-2,3-DPA derivatives 1a–1n and one (Z)-2,3-DPA-derivative 1l′ using a Perkin reaction with phenylacetic acid and appropriate substituted benzaldehydes. In our mushroom tyrosinase assay, 1c showed higher tyrosinase inhibitory activity (76.43 ± 3.53%, IC50 = 20.04 ± 1.91 µM) with than the other 2,3-DPA derivatives or kojic acid (21.56 ± 2.93%, IC50 = 30.64 ± 1.27 μM). Our mushroom tyrosinase inhibitory results were supported by our docking study, which showed compound 1c (−7.2 kcal/mole) exhibited stronger binding affinity for mushroom tyrosinase than kojic acid (−5.7 kcal/mole). In B16F10 melanoma cells (a murine cell-line), 1c showed no cytotoxic effect up to a concentration of 25 μM and exhibited greater tyrosinase inhibitory activity (68.83%) than kojic acid (49.39%). In these cells, arbutin (a well-known tyrosinase inhibitor used as the positive control) only inhibited tyrosinase by 42.67% even at a concentration of 400 μM. Furthermore, at 25 µM, 1c reduced melanin contents in B16F10 melanoma cells by 24.3% more than kojic acid (62.77% vs. 38.52%). These results indicate 1c is a promising candidate treatment for pigmentation-related diseases and potential skin whitening agents. 相似文献
3.
《Bioorganic & medicinal chemistry》2014,22(15):3994-4000
Tyrosinase is involved in the synthesis of melanin in the skin and hair as well as neuromelanin in the brain. This rate limiting enzyme catalyzes two critical steps (reactions) in melanogenesis; the hydroxylation of tyrosine to form DOPA and the subsequent oxidation of DOPA into dopaquinone. Several new aminophenol derivatives have been synthesized based on structure–activity relationship studies of N-(4-hydroxyphenyl)retinamide (1), a derivative of retinoic acid. In order to find new tyrosinase inhibitors, we investigated the effects of these p-aminophenols, including p-decylaminophenol (3), on the activity of mushroom tyrosinase. Compound 3 was the most potent agent, showing significant inhibition as compared with control. The inhibitory effects of 3 on tyrosinase activities were greater than seen with kojic acid, a well-known potent inhibitor of tyrosinase activity, which also causes adverse effects, including rash and dermatitis. A Lineweaver–Burk kinetic analysis of inhibition showed that 3 suppresses tyrosinase activity in a non-competitive fashion for both substrates, tyrosine and DOPA. These results suggest that 3 might be a useful alternative to kojic acid as a tyrosinase inhibitor. 相似文献
4.
《Bioorganic & medicinal chemistry letters》2020,30(15):127276
A new series of alkynyl glycoside analogues were designed and synthesized from cheap and a commercially available sugar by introduction of various alkynyl and alkyl groups at C-1 and C-6 positions of the sugar ring. The inhibitory abilities of alkynyl glycosides were investigated in vitro on mushroom tyrosinase for the catalysis of l-Tyrosine and l-DOPA as substrates and comparing with arbutin and kojic acid. Non-terminal alkyne compound 2d showed excellent tyrosinase inhibitory activity (IC50 54.0 μM) against l-Tyrosine comparable to arbutin (IC50 1.46 mM) while 2b exhibited potent activities (IC50 34.3 μM) against L-DOPA higher than kojic acid (IC50 0.11 mM) and arbutin (IC50 13.3 mM). Kinetic studies revealed that compound 2d was a non-competitive inhibitor with the best Ki value of 21 μM and formed an irreversible receptor complex with mushroom tyrosinase. The SARs results showed that the type of alkyne and alkyl groups at position C-6 on sugar and the stereoisomer played an important role in determining their inhibitory activities. The potent activity of alkynyl glycosides identified in this study highlight the importance of this scaffold and these compounds are very modestly potent to the development of new class for tyrosinase inhibitor. 相似文献
5.
Hydrogen peroxide (H2O2) inactivates mushroom tyrosinase in a biphasic manner, with the rate being faster in the first phase than in the second one. The inactivation of the enzyme is dependent on H2O2 concentration (in the range of 0.05–5.0 mM), but independent of the pH (in the range of 4.5–8.0). The rate of inactivation of mushroom tyrosinase by H2O2 is faster under anaerobic conditions (nitrogen) than under aerobic ones (air). Substrate analogues such as L-mimosine, L-phenylalanine, p-fluorophenylalanine and sodium benzoate protect the enzyme against inactivation by H2O2. Copper chelators such as tropolone and sodium azide also protect the enzyme. Under identical conditions, apotyrosinase is not inactivated by H2O2, unlike holotyrosinase. The inactivation of mushroom tyrosinase is not accelerated by an OH?dot generating system (Fe2+-EDTA-H2O2) nor is it protected by OHdot scavengers such as mannitol, urate, sodium formate and histidine. Exhaustive dialysis or incubation with catalase does not restore the activity of H2O2-inactivated enzyme. The data suggest that Cu2+ at the active site of mushroom tyrosinase is essential for the inactivation by H2O2. The inactivation does not occur via the OHdot radical in the bulk phase but probably via an enzyme-bound OHdot. 相似文献
6.
《Journal of enzyme inhibition and medicinal chemistry》2013,28(6):874-883
AbstractA series of umbelliferone analogues were synthesized and their inhibitory effects on the DPPH and mushroom tyrosinase were evaluated. The results showed that some of the synthesized compounds exhibited significant mushroom tyrosinase inhibitory activities. Especially, 2-oxo-2-[(2-oxo-2H-chromen-7-yl)oxy]ethyl-2,4-dihydroxybenzoate (4e) bearing 2,4-dihydroxy substituted phenyl ring exhibited the most potent tyrosinase inhibitory activity with IC50 value 8.96?µM and IC50 value of kojic acid is 16.69. The inhibition mechanism analyzed by Lineweaver–Burk plots revealed that the type of inhibition of compound 4e on tyrosinase was non-competitive. The docking study against tyrosinase enzyme was also performed to determine the binding affinity of the compounds. The compounds 4c and 4e showed the highest binding affinity with active binding site of tyrosinase. The initial structure activity relationships (SARs) analysis suggested that further development of such compounds might be of interest. The statistics of our results endorses that compounds 4c and 4e may serve as a structural template for the design and development of novel tyrosinase inhibitors. 相似文献
7.
Tyrosinase inhibitors have become increasingly important as whitening agents and for the treatment of pigmentary disorders. In this study, the synthesis of kojic acid derivatives having 2-substituted-3-hydroxy-6-hyroxymethyl/chloromethyl/methyl/morpholinomethylpiperidinyl- methyl/pyrrolidinylmethyl-4H-pyran-4-one structure (compounds 1–30) with inhibitory effects on tyrosinase enzyme were described. One-pot Mannich reaction was carried out by using kojic acid/chlorokojic acid/allomaltol and substituted benzylpiperazine derivatives in presence of formaline. Subsequently, cyclic amine (morpholine, piperidine and pyrrolidine) derivatives of the 6th-position of chlorokojic acid were obtained with nucleophilic substitutions in basic medium. The structures of new compounds were identified by FT-IR, 1H- and 13C NMR, ESI-MS and elemental analysis data. The potential mushroom tyrosinase inhibitory activity of the compounds were evaluated by the spectrophotometric method using l-DOPA as a substrate and kojic acid as the control agent. The potential inhibitory activity was also investigated in silico using molecular docking simulation method. Tyrosinase inhibitory action was significantly more efficacious for several compounds (IC50: 86.2–362.1 µM) than kojic acid (IC50: 418.2). Compound 3 bearing 3,4-dichlorobenzyl piperazine moiety was proven to have the highest inhibitory activity. The results of docking studies showed that according to the predicted conformation of compound 3 in the enzyme binding site, hydroxymethyl group provides a metal complex with copper ions and enzyme. Thus, this interaction explain the high inhibitory activities of the compounds 1, 3 and 4 possessing hydroxymethyl substituent supporting the mushroom assay results with docking studies. In accordance with the results, it is suggested that Mannich bases of kojic acid bearing substituted benzyl piperazine groups (compounds 1, 3, 4, 11, 13, 14, 23, 24, 28, and 29) could be promising antityrosinase agents. Additionally, considering the relationship between tyrosinase inhibitory activity results and molecular docking, a new tyrosinase inhibition mechanism can be proposed. 相似文献
8.
《Bioorganic & medicinal chemistry letters》2020,30(1):126722
The inhibition of tyrosinase is an established strategy for treating hyperpigmentation. Our previous findings demonstrated that cinnamic acid and benzoic acid scaffolds can be effective tyrosinase inhibitors with low toxicity. The hydroxyl substituted benzoic and cinnamic acid moieties of these precursors were incorporated into new chemotypes that displayed in vitro inhibitory effect against mushroom tyrosinase. The most active compound, (2-(3-methoxyphenoxy)-2-oxoethyl (E)-3-(4-hydroxyphenyl) acrylate) 6c, inhibited tyrosinase with an IC50 of 5.7 µM, while (2-(3-methoxyphenoxy)-2-oxoethyl 2, 4-dihydroxybenzoate) 4d had an IC50 of 23.8 µM. In comparison, the positive control, kojic acid showed tyrosinase inhibition with an IC50 = 16.7 µM. Analysis of enzyme kinetics revealed that 6c and 4d displayed noncompetitive reversible inhibition of the second tyrosinase enzymatic reaction with Ki values of 11 µM and 130 µM respectively. In silico docking studies with mushroom tyrosinase (PDB ID 2Y9X) predicted possible binding modes in the catalytic site for these active compounds. The phenolic para-hydroxy group of the most active compound 6c is predicted to interact with the catalytic site Cu++ ion. The methoxy part of this compound is predicted to form a hydrogen bond with Arg 268. Compound 6c had no observable toxic effects on cell morphology or cell viability at the highest tested concentration of 91.4 µM. When dosed at 91.4 µM onto B16F10 melanoma cells in vitro 6c showed anti-melanogenic effects equivalent to kojic acid at 880 µM. 6c displayed no PAINS (pan-assay interference compounds) alerts. Our results show that compound 6c is a more potent tyrosinase inhibitor than kojic acid and is a candidate for further development. Our exposition of the details of the interactions between 6c and the catalytic pocket of tyrosinase provides a basis for rational design of additional potent inhibitors of tyrosinase, built on the cinnamic acid scaffold. 相似文献
9.
Su Jeong Kim Jungho Yang Sanggwon Lee Chaeun Park Dongwan Kang Jinia Akter Sultan Ullah Yeon-Jeong Kim Pusoon Chun Hyung Ryong Moon 《Bioorganic & medicinal chemistry》2018,26(14):3882-3889
Thirteen (Z)-4-(substituted benzylidene)-3-phenylisoxazol-5(4H)-ones were designed to confirm the geometric effect of the double bond of the β-phenyl-α, β-unsaturated carbonyl scaffold on tyrosinase inhibitory activity. Compounds 1a–1m, which all possessed the (Z)-β-phenyl-α, β-unsaturated carbonyl scaffold, were synthesized using a tandem reaction consisting of an isoxazolone ring formation and a Knoevenagel condensation, and three starting materials, ethyl benzoylacetate, hydroxylamine and benzaldehydes. Some of the compounds showed inhibitory activity against mushroom tyrosinase as potent as compounds containing the “(E)”-β-phenyl-α, β-unsaturated carbonyl scaffold. Compounds 1c and 1m showed greater inhibitory activity than kojic acid: IC50?=?32.08?±?2.25?μM for 1c; IC50?=?14.62?±?1.38?μM for 1m; and IC50?=?37.86?±?2.21?μM for kojic acid. A kinetic study indicated that 1m inhibited tyrosinase in a competitive manner and that it probably binds to the enzyme’s active site. In silico docking simulation supported binding of 1m (?7.6?kcal/mol) to the active site of tyrosinase with stronger affinity than kojic acid (?5.7?kcal/mol). Similar results were obtained using cell-based assays, and in B16F10 cells, compound 1m dose-dependently inhibited tyrosinase activity and melanogenesis. These results indicate the anti-melanogenic effect of compound 1m is due to the inhibition of tyrosinase and (Z)-isomer of the β-phenyl-α, β-unsaturated carbonyl scaffold can, like its congener the (E)-isomer, act as an excellent scaffold for tyrosinase inhibition. 相似文献
10.
The lipophilicity of kojic acid [5-hydroxy-2-(hydroxymethyl)-4H-pyran-4-one] was improved by esterifying kojic acid with either divinyl adipate, vinyl hexanoate, vinyl octanoate or vinyl decanoate using protease from Bacillus subtilis for 7 d. 1H-NMR and 13C-NMR showed that the primary hydroxyl group at the C-7 position of kojic acid was regioselectively esterified to afford 7-O-vinyl adipoyl kojic acid, 7-O-hexanoyl kojic acid, 7-O-octanoyl kojic acid and 7-O-decanoyl kojic acid (13–27% yield). The kojic acid esters had radical scavenging activities, inhibited tyrosinase activity and was biodegradable. 相似文献
11.
Mohammad Mahdavi Arsalan Ashtari Mahsima Khoshneviszadeh Sara Ranjbar Ameneh Dehghani Tahmineh Akbarzadeh Bagher Larijani Mehdi Khoshneviszadeh Mina Saeedi 《化学与生物多样性》2018,15(7)
A novel series of benzimidazole‐1,2,3‐triazole hybrids containing substituted benzyl moieties were designed, synthesized and evaluated for their inhibitory activity against mushroom tyrosinase. The results indicated that 2‐(4‐{[1‐(3,4‐dichlorobenzyl)‐1H‐1,2,3‐triazol‐4‐yl]methoxy}phenyl)‐1H‐benzimidazole ( 6g ) and 2‐(4‐{[1‐(4‐bromobenzyl)‐1H‐1,2,3‐triazol‐4‐yl]methoxy}phenyl)‐1H‐benzimidazole ( 6h ) exhibited effective inhibitory activity with IC50 values of 9.42 and 10.34 μm , respectively, comparable to that of kojic acid as the reference drug (IC50 = 9.28 μm ). Kinetic study of compound 6g confirmed mixed‐type inhibitory activity towards tyrosinase indicating that it can bind to free enzyme as well as enzyme‐substrate complex. Also, molecular docking analysis was performed to determine the binding mode of the most potent compounds ( 6g and 6h ) in the active site of tyrosinase. Consequently, 6g and 6h derivatives might serve as promising candidates in cosmetics, medicine or food industry, and development of such compounds may be of an interest. 相似文献
12.
Dihydroxybenzoic acids (DBA), such as 3,4-DRA, 3,5-DBA, and 2,4-DBA—at all concentrations tested—inhibited the rate of DL-DOPA oxidation to dopachrome (λmax = 475 nm) by mushroom tyrosinase. 2,3-DBA and 2,5-DBA at relatively low concentration had a synergistic effect on the reaction, whereas at relatively high concentrations they inhibited the rate of DL-DOPA oxidation. The synergistic effect of 0.6-13.3 mM 2,3-DRA on the rate of DL-DOPA oxidation to dopachrome (λmax = 475 nm) was found to be due to the ability of 2,3-DBA-o-quinone (formed by the oxidation of 2,3-DBA by mushroom tyrosinase or by sodium periodate) to oxidize DL-DOPA to dopachrome (via dopaquinone) non-enzymatically. A similar explanation is likely to be valid for the synergism exerted by 2,5-DBA on the rate of DL-DOPA oxidation by mushroom tyrosinase. 相似文献
13.
A series of kojic acid-derived compounds 6a-p bearing aryloxymethyl-1H-1,2,3-triazol-1-yl moiety were designed by modifying primary alcoholic group of kojic acid as tyrosinase inhibitors. The target compounds 6a-p were synthesized via click reaction. All compounds showed very potent anti-tyrosinase activity (IC50s = 0.06–6.80 µM), being superior to reference drug, kojic acid. In particular, the naphthyloxy analogs 6o and 6p were found to be 31–155 times more potent than kojic acid. The metal-binding study of selected compound 6o revealed that the prototype compound possesses metal-chelating ability, particularly with Cu2+ ions. The promising compounds 6o and 6p had acceptable safety profile as demonstrated by cytotoxicity assay against melanoma (B16) cell line and Human Foreskin Fibroblast (HFF) cells. 相似文献
14.
F Schved V Kahn 《Pigment cell research / sponsored by the European Society for Pigment Cell Research and the International Pigment Cell Society》1992,5(2):58-64
Dihydroxybenzoic acids (DBA), such as 3,4-DBA, 3,5-DBA, and 2,4-DBA--at all concentrations tested--inhibited the rate of DL-DOPA oxidation to dopachrome (lambda max = 475 nm) by mushroom tyro0sinase. 2,3-DBA and 2,5-DBA at relatively low concentration had a synergistic effect on the reaction, whereas at relatively high concentrations they inhibited the rate of DL-DOPA oxidation. The synergistic effect of 0.6-13.3 mM 2,3-DBA on the rate of DL-DOPA oxidation to dopachrome (lambda max = 475 nm) was found to be due to the ability of 2,3-DBA-o-quinone (formed by the oxidation of 2,3-DBA by mushroom tyrosinase or by sodium periodate) to oxidize DL-DOPA to dopachrome (via dopaquinone) non-enzymatically. A similar explanation is likely to be valid for the synergism exerted by 2,5-DBA on the rate of DL-DOPA oxidation by mushroom tyrosinase. 相似文献
15.
Ahn SM Rho HS Baek HS Joo YH Hong YD Shin SS Park YH Park SN 《Bioorganic & medicinal chemistry letters》2011,21(24):7466-7469
A novel kojic acid derivative containing a trolox moiety, (±)-5-hydroxy-4-oxo-4H-pyran-2-yl methyl 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylate (3a), was synthesized. The two biologically active compounds, namely, kojic acid and trolox, were conjugated via an ester bond as they are expected to behave synergistically. The antioxidant activity and the tyrosinase inhibitory activity of this novel kojic acid derivative on melanogenesis were evaluated. Compound 3a exhibited potent tyrosinase inhibitory activity and radical scavenging activity. Limited structure–activity relationship (SAR) investigations indicated that the tyrosinase inhibitory activities may originate from the kojic acid moiety, and the radical scavenging activity may be due to the phenolic hydroxyl group of trolox. Compound 3a also exhibited potent depigmenting activity in a cell-based assay. The limited SAR investigations revealed that the depigmenting activity of 3a may be due to the synergistic activities of kojic acid and its trolox moiety. 相似文献
16.
Hui-Min Wang Chung-Yi Chen Chun-Yen Chen Mei-Ling Ho Yi-Ting Chou Hou-Chien Chang Chih-Hung Lee Chau-Zen Wang I-Ming Chu 《Bioorganic & medicinal chemistry》2010,18(14):5241-5247
Tyrosinase is the first and rate limiting enzyme in the synthesis of melanin pigments for coloring hair, skin, and eyes. As reported in this study, a natural product, (?)-N-formylanonaine isolated from the leaves of Michelia alba D.C. (Magnolianceae), was found to inhibit mushroom tyrosinase with an IC50 of 74.3 μM and to have tyrosinase and melanin reducing activities in human epidermal melanocytes without apparent cytotoxicity to human cells, superior to the known tyrosinase inhibitors, such as kojic acid and 1-phenyl-2-thiourea (PTU). Based on homology modeling, the compound binds the active site by coordinating with two Cu2+ ions. In addition, the compound had antioxidation activities in tests for scavenging 1,1-diphenyl-2-picrylhydrazyl (DPPH), reducing power, and chelating metal ions. To our knowledge, this is the first study to reveal the bioactivities of (?)-N-formylanonaine from this plant species. 相似文献
17.
《Bioorganic & medicinal chemistry》2019,27(17):3929-3937
Targeting of tyrosinase has proven to be the best means of identifying safe, efficacious, and potent tyrosinase inhibitors for whitening skin. We designed and synthesized ten NAB (N-(acryloyl)benzamide) derivatives (1a–1j) using the Horner-Wadsworth-Emmons olefination of diethyl (2-benzamido-2-oxoethyl)phosphonate and appropriate benzaldehydes. A mushroom tyrosinase inhibitory assay showed compounds 1a (36.71 ± 2.14% inhibition) and 1j (25.99 ± 2.77% inhibition) inhibited tyrosinase more than the other eight NAB derivatives and kojic acid (21.56 ± 2.93% inhibition), and docking studies indicated 1a (−6.9 kcal/mole) and 1j (−7.5 kcal/mole) had stronger binding affinities for tyrosinase than kojic acid (−5.7 kcal/mole). At a concentration of 25 μM, 1a and 1j were nontoxic in B16F10 melanoma cells and exhibited stronger tyrosinase inhibition (59.70% and 76.77%, respectively) than kojic acid (50.30% inhibition) or arbutin (41.78% inhibition at 400 μM). Similarly, in B16F10 melanoma cells, compounds 1a and 1j at 25 μM decreased total melanin content by 47.97% and 61.77%, respectively (kojic acid; 38.98%). Similarities between inhibitions of tyrosinase activity and melanin contents suggested the anti-melanogenic effects of 1a and 1j were due to tyrosinase inhibition. The excellent DPPH scavenging activity of 1j suggests it might enhance in vivo effect on melanin contents. The study suggests compound 1j offers a potential starting point for the development of safe, potent tyrosinase inhibitors. 相似文献
18.
《Phytochemistry》1986,25(2):333-337
Mushroom tyrosinase is affected by hydroxylamine (NH2OH) in several ways. At relatively low concentrations (up to 33 mM) NH2OH shortens the lag period of tyrosine hydroxylation. The o-dihydroxyphenolase activity of mushroom tyrosinase is slightly stimulated by short exposure to relatively low concentrations ofNH2OH (1.5 mM). Relatively high concentrations ofNH2OH (above 20 mM) inhibit the o-dihydroxyphenolase activity of the enzyme and lowers the extent of final pigment production. Preincubation of mushroom tyrosinase with different concentrations ofNH2OH for different times results in the inactivation of the enzyme. The rate of inactivation occurred much faster under anaerobic than under aerobic conditions. It was also found that NH2OH changes the spectra of o-quinones prepared chemically or of products formed during the oxidation of o-dihydroxyphenols by mushroom tyrosinase. These spectral changes were attributed to the formation of oximes (mono- or dioximes) as a result of an interaction between o-quinones and NH2OH. The apparent inhibition exerted by NH2OH on the o-dihydroxyphenolase activity of mushroom tyrosinase is, in part, due to spectral changes in pigmented product formation and, in part, due to the inactivation of the enzyme by NH2OH. 相似文献
19.
《Biochimica et Biophysica Acta (BBA)/Molecular Cell Research》1994,1222(1):95-100
Leucine enkephalin (1 mM) was reacted with mushroom tyrosinase under reductive conditions (ascorbic acid, 50 mM). Reaction products were isolated by high-performance liquid chromatography and identified using electrospray ionization mass spectrometry. The products of the reaction were found to be hydroxylated at the Tyr1 moiety of the peptide. The major product was a monohydroxylated derivative of leucine enkephalin ([HO-Tyr1]LE) and the minor product of the reaction was a dihydroxylated derivative ([(HO)2-Tyr1]LE). The affinity of [HO-Tyr1]LE to receptors in rat brain homogenate was compared to that of leucine enkephalin itself. Hydroxylation of LE was found to decrease receptor affinity to both μ and δ opioid receptor sites by a factor of about 20. 相似文献
20.
Soo Sung Kang Hyoung Ja Kim Changbae Jin Yong Sup Lee 《Bioorganic & medicinal chemistry letters》2009,19(1):188-191
Melanogenesis is a physiological process that results in the production of melanin pigment. However, excessive accumulations of epidermal pigmentation can cause various hyperpigmentary disorders such as, melasma and age spots. Kojic acid and hydroxylated cinnamic acid derivatives are known to inhibit tyrosinase, a key component of melanin biosynthesis. Pyronyl-acrylic acid esters 3a–i, which share structural features of kojic acid and hydroxylated cinnamic acid, were prepared and their abilities to inhibit tyrosinase and melanin production were evaluated. Of the esters synthesized, 3e and 3h, which derived from diethylene glycol moieties were found to inhibit melanin production by ca. 20% at 20 μg/ml, whereas kojic acid at 200 μg/ml inhibited melanin production by 15.8%. 相似文献