25520-73-4Relevant articles and documents
Protection of mesopore-adsorbed organic matter from enzymatic degradation
Zimmerman, Andrew R.,Chorover, Jon,Goyne, Keith W.,Brantley, Susan L.
, p. 4542 - 4548 (2004)
Synthetic mesoporous alumina and silica minerals with uniform pore geometries, and their nonporous analogues, were used to test the role of mineral mesopores (2-50 nm diameter) in protecting organic matter from enzymatic degradation in soils and sediments
Enantioselectively catalyzed oxidation of 3,4-dihydroxy-L-phenylalanine by N-lauroyl L or D-histidine-Cu(II) complex in CTABr micelles
Yamada,Shosenji,Otsubo,Ono
, p. 2649 - 2652 (1980)
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Highly sensitive voltammetric sensor based on NiO nanoparticle room temperature ionic liquid modified carbon paste electrode for levodopa analysis
Fouladgar, Masoud,Karimi-Maleh, Hassan,Gupta, Vinod Kumar
, p. 78 - 83 (2015)
This paper describes the development of 1-methyl-3-butylimidazolium chloride ionic liquid-NiO nanoparticle modified carbon paste electrode (MBICl/NiO/NPs/CPE) for the voltammetric determination of levodopa (l-DOPA) in real samples. We describe the synthes
Reactivity of dinuclear copper(II) complexes towards melanoma cells: Correlation with its stability, tyrosinase mimicking and nuclease activity
Nunes, Cléia Justino,Borges, Beatriz Essenfelder,Nakao, Lia Sumie,Peyroux, Eugénie,Hardré, Renaud,Faure, Bruno,Réglier, Marius,Giorgi, Michel,Prieto, Marcela Bach,Oliveira, Carla Columbano,Da Costa Ferreira, Ana M.
, p. 49 - 58 (2015)
In this work, the influence of two new dinuclear copper(II) complexes in the viability of melanoma cells (B16F10 and TM1MNG3) was investigated, with the aim of verifying possible correlations between their cytotoxicity and their structure. One of the comp
Tyrosinase inhibitory polyphenols from roots of Morus Ihou
Jeong, Seong Hun,Ryu, Young Bae,Curtis-Long, Marcus J.,Ryu, Hyung Won,Baek, Yoon Su,Kang, Jae Eun,Lee, Woo Song,Park, Ki Hun
, p. 1195 - 1203 (2009)
Twelve polyphenols (1-12) possessing tyrosinase inhibitory properties were isolated from the methanol (95%) extract of Morus Ihou. The isolated compounds consisted of four flavanones (1 -4), four flavones (5-8), and four phenylbenzofuranes (9-12). Moracin derivative 12 proved to be new a compound which was fully characterized. Compounds 1-12 were evaluated for both monophenolase and diphenolase (the two steps catalyzed by tyrosinase) inhibition to identify the structural characteristics required for mushroom tyrosinase inhibition. We observed that all parent compounds (1, 5, and 9) possessing an unsubstituted resorcinol group were highly effective inhibitors of monophenolase activity (IC50 values of 1.3, 1.2, and 7.4 μM). The potency of the inhibitors diminished with alkyl substitution on either the aromatic ring or the hydroxyl functions. Interestingly, flavone 5 was shown to possess only monophenolase inhibitory activity, but flavanone 1 and phenylbenzofuran 9 inhibited diphenolase as well as monophenolase significantly. The inhibitory mode of these species was also dependent upon the skeleton: phenylbenzofuran 9 manifested a simple competitive inhibition mode for monophenolase and diphenolase; on the other hand flavanone 1 (monophenolase, K3 = 0.1966 min-1 μM-1 k4= 0.0082 min ~1, and Kiapp = 0.0468 μM; diphenolase, k3 = 0.0014 min-1 μM-1 k4 = 0.0013 min-1, and Kiapp = 0.8996 μM) and flavone 5 both showed time-dependent inhibition against monophenolase. Compound 1 operated according to the simple reversible slow binding model whereas compound 5 operated under the enzyme isomerization model.
Tyrosinase inactivation in its action on dopa
Mu?oz-Mu?oz,Acosta-Motos,Garcia-Molina,Varon,Garcia-Ruíz,Tudela,Garcia-Cánovas,Rodríguez-López
, p. 1467 - 1475 (2010)
Under aerobic or anaerobic conditions, tyrosinase undergoes a process of irreversible inactivation induced by its physiological substrate l-dopa. Under aerobic conditions, this inactivation occurs through a process of suicide inactivation involving the fo
Stereoselective Electrone Transfer between Chiral Catecholamines and Iron(III) Complex Ions Anchored to Asymmetric Polymers. A Kinetic and Conformational Investigation
Pispisa, Basilio,Palleschi, Antonio,Barteri, Mario,Nardini, Stefanella
, p. 1767 - 1775 (1985)
The oxydation of L-dopa (3,4-dihydroxyphenylalanine) and L-adrenaline (epinephrine) by + complex ions anchored to poly(L-glutamate) (FeTL) or poly(D-glutamate) (FeTD) was studied at pH 7 (tetpy = 2,2':6',2'':6'',2'''-tetrapyridy
Coumaric acid derivatives as tyrosinase inhibitors: Efficacy studies through in silico, in vitro and ex vivo approaches
Fernandes, Jo?o Paulo S.,Ferrarini, Márcio,Mercaldi, Vitória Gallo,Nazato, Lucas Idacir Sbrugnera,Padovani, Giovana,Sufi, Bianca da Silva,Varela, Marina Themoteo
, (2020/08/06)
p-Coumaric acid is a known inhibitor of tyrosinase, an enzyme involved in the initial steps of the melanin synthesis in human and other species. However, its low lipophilicity impairs its penetration through skin and efficacy as antimelanogenic agent indeed. Accordingly, this paper reports the assessment of several coumaric acid derivatives as tyrosinase inhibitors and antimelanogenic agents in in vitro, in silico and ex vivo assays. The compounds were designed with modifications in the aromatic and acid moieties of p-coumaric acid, being the coumarate esters the most promising derivatives. The compounds showed higher tyrosinase inhibitory activity (pIC50 3.7–4.2) than the parent acid, being compounds 1d, 1e and 1f the most potent inhibitors. Docking analysis showed that these esters are competitive inhibitors per se, and act independently of a redox mechanism as suggested by DPPH assays. Moreover, the esters showed efficacy in reducing the melanin deposition in human skin fragments at 0.1% concentration, especially compound 1e. In summary, there is an important equilibria between tyrosinase affinity and lipophilicity that must be considered to get effective antimelanogenic agents with adequate permeability in the skin.