• Natural Product Sciences
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• v.10 no.6
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• pp.272-276
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• 2004

During the course of our screening for bioactive metabolites from marine sponges, EZZ, the inseparable 1:1 mixture of (8E,13Z,20Z)-strobilinin and (7E,13Z,20Z)-felixinin has been found to deliver significant cytotoxicity against some cancer cell lines. In this study, the antioxidant activity of EZZ was first time evaluated by a series of antioxidant assays. It was found that EZZ was weak in scavenging the stable free radical 1,1-diphenyl-2-picrylhyrazyl (DPPH), but it was comparable to ascorbic acid in scavenging ABTS and superoxide radicals. In addition, EZZ could protect DNA from hydroxyl radical-induced strand cleavage. The findings of the present study suggest that EZZ possess certain antioxidant activity, which might help to prevent occurrence of cancer by alleviating the oxidative stress in cells.

• Bulletin of the Korean Chemical Society
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• v.21 no.9
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• pp.923-928
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• 2000

[FeIII(BBA)DBC]ClO4 as a new functional model for catechol dioxygenases has been synthesized, where BBA is a bis(benzimidazolyl-2-methyl)amine and DBC is a 3,5-di-tert-butylcatecholate dianion.The BBA complex has a structuralfeature that iron cent er has a five-coordinate geometry similar to that of catechol dioxygenase-substrate complex.The BBA complex exhibits strong absorptionbands at 560 and 820 nm in CH3CN which are assigned to catecholate to Fe(III) charge transfer transitions. It also exhibits EPR signals at g = 9.3 and 4.3 which are typical values for the high-spin FeIII (S = 5/2) complex with rhombicsymmetry. Interestingly, the BBA complex reacts with O2 within an hour to afford intradiol cleavage (35%) and extradiol cleavage (60%) products. Surprisingly, a green color intermediate is observed during the oxygenation process of the BBA com-plex in CH3CN. This green intermediate shows a broad isotropic EPR signal at g = 2.0. Based on the variable temperature EPR study, this isotropic signalmight be originated from the [Fe(III)-peroxo-catecholate] species havinglow-spin FeIII center, not from the simple organic radical. Consequently,it allows O2 to bind to iron cen-ter forming the Fe(III)-superoxide species that converts to the Fe(III)-peroxide intermediate. These present data can lead us tosuggest that the oxygen activation mechanism take place for the oxidative cleavingcatechols of the five-coordinate model systems for catechol dioxygenases.

• Journal of Fashion Business
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• v.12 no.6
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• pp.23-33
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• 2008

The physico-chemical characteristics by bleaching treatments were assessed by several instrumental analyses such as surface morphology, chemical structural change, color change as well as tensile strength. The change of morphological characteristic was observed through scanning electron microscope(SEM). The observation of the fine structure on hair surface by SEM showed the bleached hair had much damaged to hair cuticle, and some of cuticle surface were worn away. To investigate the chemical structural changes in hair keratin, the cross-sections of hair samples were directly analysed using Fourier transform infrared microspectroscopy(FT-IRM). The results showed the cysteic acid S=O band intensity was distinctively increased by performing the bleaching treatment. The cleavage of cystine was appeared to proceed primarily through the sulfur-sulfur (-S-S-) fission whereby cysteic acid was formed as a principal oxidation products. The distribution of amide I band in hair keratin was determined by attenuated total reflectance(ATR) FT-IR mapping image. The results showed that the outer side of hair cortex was more damaged than the inner side of the hair cortex. Also, during chemical bleaching of the hair with alkaline peroxide, the hair was turned to reddish yellow due to the oxidative degradation of eumelanin. This means the eumelanin is more unstable than pheomelanin in chemical oxidation. With bleaching, the tensile strength was also reduced as a results of the chemical oxidation.