4430-97-1Relevant articles and documents
CHROMATOGRAPHIC AND SPECTROSCOPIC INVESTIGATION OF THE PRODUCTS OF OXIDATION OF TYROSINE WITH OZONE.
Ignatenko,Cherenkevich,Komyak
, p. 798 - 802 (1984)
It has been shown that ozone in low concentrations readily oxidizes aromatic amino acids both in solution and when constituents of proteins resulting in the formation of a whole series of oxidation products. Since the oxidation products are physiologically active it was of interest to study them further. In the present work the main molecular products obtained by oxidation of tyrosine with ozone are established, and possible mechanisms of their formation discussed.
Electrochemistry of Chemisorbed Molecules. 4.The Effect of Chirality on the Orientation and Electrochemical Oxidation of l - and dl-DOPA
Chila, Victor K. F.,Sorilaga, Manuel P.,Hubbard, Arthur T.,Anderson, Stanley E.
, p. 232 - 235 (1983)
The influence of chirality on the orientation and electrochemical oxidation of l- and dl-DOPA chemisorbed on Pt electrodes has been studied.Measurements were made in 1 M HClO4 with thin-layer electrochemical methods.In the flat orientation, Γ (the packing
Biochemical characterization of two differentially expressed polyphenol oxidases from hybrid poplar
Wang, Jiehua,Constabel, C. Peter
, p. 115 - 121 (2003)
Two polyphenol oxidase isoforms with distinct expression patterns were identified in hybrid poplar (Populus trichocarpax P. deltoides). PPO-1, corresponding to the previously cloned PtdPPO (Constabel et al., Plant Physiol. 124: 285-295) was primarily leaf
Genetically encoded dihydroxyphenylalanine coupled with tyrosinase for strain promoted labeling
George, Augustine,Indhu, Mohan,Ashokraj, Sundarapandian,Shanmugam, Ganesh,Ganesan, Ponesakki,Kamini, Numbi Ramudu,Ayyadurai, Niraikulam
supporting information, (2021/11/08)
Protein modifications through genetic code engineering have a remarkable impact on macromolecule engineering, protein translocation, protein–protein interaction, and cell biology. We used the newly developed molecular biology approach, genetic code engineering, for fine-tuning of proteins for biological availability. Here, we have introduced 3, 4-dihydroxy-L-phenylalanine in recombinant proteins by selective pressure incorporation method for protein-based cell labeling applications. The congener proteins treated with tyrosinase convert 3, 4-dihydroxy-L-phenylalanine to dopaquinone for strain-promoted click chemistry. Initially, the single-step Strain-Promoted Oxidation-Controlled Cyclooctyne-1,2-quinone Cycloaddition was studied using tyrosinase catalyzed congener protein and optimized the temporally controlled conjugation with (1R,8S,9s)-Bicyclo[6.1.0]non-4-yn-9-ylmethanol. Then, the feasibility of tyrosinase-treated congener annexin A5 with easily reactive quinone functional moiety was conjugated with fluorescent tag dibenzocyclooctyne-PEG4-TAMRA for labeling of apoptotic cells. Thus, the congener proteins-based products demonstrate selective cell labeling and apoptosis detection in EA.hy926 cells even after the protein modifications. Hence, genetic code engineering can be coupled with click chemistry to develop various protein-based fluorescent labels.
SKIN-WHITENING COSMETIC COMPOSITION COMPRISING LACTOBACILLUS RHAMNOSUS LM1011 HAVING IMMUNOSTIMULATING ACTIVITY
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Paragraph 0009, (2020/05/13)
The present invention relates to a cosmetic composition for skin whitening comprising novel Lactobacillus rhamnosus LM1011 as an active ingredient. More specifically, the present invention provides a cosmetic composition for skin whitening, comprising novel Lactobacillus rhamnosus LM1011 as an active ingredient, and reducing melanin production by regulating tyrosinase activity.(AA) L-tyrosine 4-hydroxy-1-phenylalanine(BB) Tyrosinase(CC) L-dopa 1-3,4-dihydroxyphenylalanine(DD) Dehydroascorbic acid(EE) Ascorbic acid(FF) Tyrosinase(GG) Dopaquinone(HH) MelaninCOPYRIGHT KIPO 2020
Inhibitory effects and molecular mechanism on mushroom tyrosinase by condensed tannins isolation from the fruit of Ziziphus jujuba Mill. var. spinosa (Bunge) Hu ex H. F. Chow
Liu, Lu-Lu,Ren, Yuan-Jing,Song, Wei,Wei, Shu-Dong,Yang, Hai-Bo
, p. 1813 - 1821 (2020/11/03)
The structure of extracted condensed tannin (CT) from the fruit of Sour jujube (Ziziphus jujuba Mill. var. spinosa (Bunge) Hu ex H. F. Chow) and the molecular mechanisms by which CT inhibits the activity of mushroom tyrosinase were investigated. The structure of CT was characterized by high performance liquid chromatography electrospray ionization mass spectrometry, and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The kinetic assays were used to detect inhibition effect, type and mechanism. UV scanning, fluorescence quenching, copper interacting, o-quinone interaction and molecular docking assays were also used to reveal the molecular mechanisms by which CT inhibit tyrosinase. The results showed the structural units of CT containing afzelechin/epiafzelechin, catechin/epicatechin, and gallocatechin/epigallocatechin. Kinetic analysis showed that CT inhibits both the monophenolase and diphenolase activities of tyrosinase and exhibits reversible, mixed type mechanism. The fruit CT interacts primarily with the copper ions and specific amino acid residue (Asn191, Thr203, Ala202, Ser206, Met201, His194, His54, Glu182 and Ile42) in the active site of tyrosinase to disturb oxidation of substrates by tyrosinase. These results suggested the sour jujube fruit is a potential natural source of tyrosinase inhibitors, and has a potential to be used in food preservation, whitening cosmetics.
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.
In vitro tyrosinase, acetylcholinesterase, and HSA evaluation of dioxidovanadium (V) complexes: An experimental and theoretical approach
Chaves, Otávio Augusto,de Oliveira, Márcia Cristina Campos,de Salles, Cristiane Martins Cardoso,Martins, Francisco Mainardi,Iglesias, Bernardo Almeida,Back, Davi Fernando
, (2019/09/06)
The present study reports the biological evaluation of vanadium(V) complexes (1–3) against three different proteins: tyrosinase, acetylcholinesterase (AChE), and human serum albumin (HSA), which were studied by spectroscopic techniques and molecular docki
Determining mushroom tyrosinase inhibition by imidazolium ionic liquids: A spectroscopic and molecular docking study
Heitz, Mark P.,Rupp, Jason W.
, p. 1971 - 1981 (2017/10/23)
The inhibition effects of imidazolium ionic liquids (ILs) on the enzyme kinetics of mushroom tyrosinase is reported. A simple UV-VIS spectrophotometric assay was used to measure the reaction kinetics of the reaction between mushroom tyrosinase and L-dopa.
Synthesis and biological evaluation of N-aryl-2-phenyl-hydrazinecarbothioamides: Experimental and theoretical analysis on tyrosinase inhibition and interaction with HSA
Sousa-Pereira, Danilo,Chaves, Otávio Augusto,dos Reis, Camilla Moretto,de Oliveira, Márcia C.C.,Sant'Anna, Carlos Maurício R.,Netto-Ferreira, José Carlos,Echevarria, Aurea
, p. 79 - 87 (2018/08/21)
A series of N-aryl-2-phenyl-hydrazinecarbothioamides have been investigated as possible inhibitors of tyrosinase, an enzyme involved in the development of melanomas. The hydrazinecarbothioamides 1–6 were synthesized from the reaction between phenylhydrazine and isothiocyanates, for which three different methods have been employed, namely stirring at room temperature, by microwave irradiation or by mechanochemical grinding. Quantitative yields were obtained for the later technique. Compound 4 showed the best value for tyrosinase inhibition (IC50 = 22.6 μM), which occurs through an uncompetitive mechanism. Molecular docking results suggested that 4 can interact via T-stacking with the substrate L-DOPA and via hydrogen bonding and hydrophobic forces with the amino acid residues Ala-79, His-243, Val-247, Phe-263, Val-282, and Glu-321. The interaction between human serum albumin (HSA) and compound 4 occurs through a ground state association and does not perturb the secondary structure of the albumin as well as the microenvironment around Tyr and Trp residues. The binding is spontaneous, moderate and occurs mainly in the Sudlow's site I. Molecular docking results suggested hydrogen bonding, hydrophobic and electrostatic interactions as the main binding forces between the compound 4 and the amino acid residues Lys-198, Trp-214, Glu-449, Leu-452, and Leu-480.
