Physico-chemical Characterization Of The Inclusion Complex Between A 2-propen-1-amine Derivative And β-cyclodextrin

Inclusion complexes and physical mixtures were prepared with isomeric mixture of E/Z (50:50) of 3-(4′-bromo-[1,1′-biphenyl]-4-yl)-3-(4- bromophenyl)-N,N-dimethyl-2-propen-1-amine (BBAP) and β-cyclodextrin (β-CD) in different proportions. In this study, theoretical calculations using Molecular Mechanics MM+ force field were applied to predict the structures of the inclusion complexes formed by interaction of BBAP and b-cyclodextrin. Circular dichroism, differential thermal analysis (DTA), X-ray diffraction and 13C CP/MAS NMR methods were used to characterize the inclusion complexes and provide information about the stoichiometry of the inclusion complexes. The combined spectroscopy techniques indicate the formation of a complex of BBAP/β-CD in the molar proportion of 1:1 and 1:2 by co-evaporation and no complexation was detected in the physical mixture of the compounds. © 2006 Sociedad Chilena de Química β-.503115127Bibby, D.C., Davies, N.M., Tucker, I.G., (2000) Int. J. Pharm., 197, p. 1Connors, K.A., (1995) J. Pharm. Sci., 84, p. 843Connors, K.A., Paulson, A., Toledo-Velasquez, D.J., (1988) J. Org. Chem., 53, p. 2123Dollo, G., Le Corre, P., Chollet, M., Chevanne, F., Bertault, M., Burgot, J.-L., Le Verge, R., (1999) J. Pharm. Sci., 88, p. 889Mucci, A., Schenetti, L., Vandelli, M.A., Ruozi, B., Forni, F., (1999) J. Chem. Research, (S), p. 414Keipert, S., Fedder, J., Bohm, A., Hanke, B., (1996) Int. J. Pharm., 142, p. 153Nigam, S., Durocher, G., (1999) J. Photochem. Photobiol. A: Chem., 103, p. 143De Souza, A.O., Sato, D.N., Aily, D.C.G., Duran, N., (1998) J. Antimicrob. Chemother., 42, p. 407Pereira, D.G., De Castro, S.L., Durán, N., (1998) Acta Tropica, 69, p. 205De Souza, A.O., Santos Júnior, R.R., Ferreira-Júlio, J.F., Rodrigues, J.A., Melo, P.S., Haun, M., Sato, D.N., Durán, N., (2001) Eur. J. Med. Chem., 36, p. 843De Souza, A.O., Hemerly, F.P., Busollo, A.C., Melo, P.S., Machado, G.M.C., Miranda, C.C., Santa-Rita, R.M., Durán, N., (2002) J. Antimicrob. Chemother., 50, p. 629De Conti, R., Gimenez, S.M.N., Haun, M., Pilli, R.A., De Castro, S.L., Durán, N., (1996) N. Eur. J. Med. Chem., 31, p. 915De Azevedo, M.B.M., Alderete, J.B., Lino, A.C.S., Loh, W., Faljoni-Alario, A., Durán, N., (2000) J. Incl. Phenom. Macrocyclic. Chem., 37, p. 67Zhou, D., Wu, Y., Xu, Q., Yang, L., Bai, C., (2000) Z. Tan. J. Incl. Phenom. Macrocyclic. Chem., 37, p. 273Ammar, H.O., Ghorab, M., El-Nahhas, S.A., Emara, I.H., Makram, T.S., (1999) Pharmazie, 54, p. 142Muñoz De La Pena, A., Ndou, T.T., Zung, J.B., Warner, I.M., (1991) J. Phys. Chem., 95, p. 3330Smith, V.K., Ndou, T.T., Warner, I.M., (1994) J. Phys. Chem., 98, p. 8627Blanco, M., Coello, J., Iturriaga, H., Maspoch, S., Pérez-Maseda, C., (2000) Anal. Chim. Acta, 407, p. 233Ohashi, M., Kasatani, K., Shinohara, H., Sato, H., (1990) J. Am. Chem. Soc., 112, p. 5824Harata, K., Uedaria, H., (1975) Bull. Chem. Soc. Jpn., 48, p. 375Schellman, J.A., (1968) Acc. Chem. Res., 1, p. 144Bettinetti, G.P., Gonzzaniga, A., Mura, P., Giordano, F., Setti, M., (1992) Drug Dev. Ind. Pharm., 18, p. 39Mura, P.P., Faucci, M.T., Parrini, P.L., Furlanetto, S., Pinzauti, S., (1999) Int. J. Pharm., 179, p. 117Cunha-Silva, L., Teixeira-Dias, J.J.C., (2002) J. Phys. Chem., 106, p. 3323Lai, S., Locci, E., Piras, A., Porcedda, S., Lai, A., Marangiu, B., (2003) Carbohydr. Res., 338, p. 222

Chromobacterium Violaceum And Its Important Metabolites--review.

C. violaceum appeared as important bacterium in different applications and mainly these aspects are related to the production of violacein. This review discusses the last reports on biosynthetic pathways, production, genetic aspects, biological activities, pathological effects, antipathogenic screening through quorum sensing, environmental effects and the products of C. violaceum with industrial interest. An important discussion is on biological applications in medicine and as industrial products such as textile and in cosmetics.55535-4

Chromobacterium Violaceum And Its Important Metabolites - Review

C. violaceum appeared as important bacterium in different applications and mainly these aspects are related to the production of violacein. This review discusses the last reports on biosynthetic pathways, production, genetic aspects, biological activities, pathological effects, antipathogenic screening through quorum sensing, environmental effects and the products of C. violaceum with industrial interest. 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Peroxidase-hydrogen Peroxide System Acting On Lignin(1)

Horseradish peroxidase (HRP)/H2O2 system, as a possible model of lignolytic enzyme, was evaluated. Aerobic peroxidation of lignin involved chemiluminescence, which arose mainly from recombination of OH radicals and carbonate ions (dissolved CO2). The peroxidase cycle followed by ultraviolet spectrophotometry and by circular dichroism pointed out the HRP-III (Fe III-O2{minus sign, dot below}) species, instead of the free-activated oxygen species, as the most reactive intermediate acting on lignin. HRP-I and HRP-II participate only in the oxidation of the phenolic moiety. The participation of HRP-III in lignin degradation open the way for more detailed studies of biological oxidation by enzyme-bound oxygen species. A general mechanism for lignin degradation by peroxidase was proposed. © 1988.342105115Kirk, (1983) Recent Advances in Lignin Biodegradation, pp. 1-11. , T. Higuchi, H.-M. Chang, T.K. Kirk, Japan: UNI Publ. Co. Ltd, Tokyo, Proc. Intern. Sem. US-Japan Cooperative Sci. ProgramKirk, (1984) Microbiological Degradation of Organic Compounds, Microbiology Series, 13, pp. 399-437. , D.T. Gibson, Marcel Dekker, Inc, New YorkKutsuki, Enoki, Gold, RIBOFLAVIN-PHOTOSENSITIZED OXIDATIVE DEGRADATION OF A VARIETY OF LIGNIN MODEL COMPOUNDS (1983) Photochemistry and Photobiology, 37, pp. 1-7Gold, Kutsuki, Morgan, OXIDATIVE DEGRADATION OF LIGNIN BY PHOTOCHEMICAL AND CHEMICAL RADICAL GENERATING SYSTEMS (1983) Photochemistry and Photobiology, 38, pp. 647-651Greene, Gould, (1984) Biochem. Biophys. Res. Commun., 118, pp. 437-443Faison, Kirk, (1984) Appl. Environ. Microbiol., 46, pp. 1140-1145Kirk, Mozuch, Tien, (1985) Biochem. J., 226, pp. 455-460Tien, Kirk, (1983) Science, 221, pp. 661-663Faison, Kirk, (1985) Appl. Environ. 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Liposome effect on the cytochrome c-catalyzed peroxidation of carbonyl substrates to triplet species

Cytochrome c exhibits peroxidase activity on diphenylacetaldehyde (DPAA) and 3-methylacetoacetone (MAA), which is greatly affected by the presence and nature of charged liposome or micelle interfaces interacting with the enzyme. The ferricytochrome c reaction with DPAA is accelerated when the enzyme is attached to negatively charged interfaces. Whatever the medium, bulk solution or negatively charged dicetylphosphate (DCP), phosphatidyl coline/phosphatidylethanolamine/cardiolipin (PC/PE/CL) liposomes, this chemiluminescent reaction is accompanied by reduction of cytochrome c to its ferrous form. In turn, MAA is oxidized by cytochrome c exclusively when bound to DCP liposomes. Contrary to DPAA oxidation, the MAA reaction is followed by bleaching of cytochrome c, reflecting damage to the hemeprotein chromophore. The cytochrome-c-catalyzed oxidation of either DPAA or MAA leads to concomitant disappearance of the enzyme charge transfer absorption band at 695 nm. This suggests that the peroxidase activity of cytochrome c involves substrate-induced loss of the methionine ligand at the iron sixth coordination position, which is favored by interaction of cytochrome c with negatively charged interfaces. Accordingly, a decrease and blue shift of the charge transfer band could be observed in cytochrome-c-containing negatively charged DCP, PC/PE/CL liposomes or lysophosphatidylethanolamine micelles in the presence of DPAA or MAA.254176354655

Sensitized Photooxygenation And Peroxidase-catalyzed Inactivation Of Xanthine Oxidase - Evidence Of Cysteine Damage By Singlet Oxygen

Xanthine oxidase (XO) has been investigated for its decreased activity in several cancerous tissues and constitutive generation of reactive oxygen species (ROS) in vivo seems to contribute significantly to its inactivation. Singlet oxygen (1O2) production has been suggested to be relevant when considering folic acid metabolism by cancer cells. Thus, the susceptibility of XO to inactivation by 1O2 generated either by the bioenergized systems folic acid/peroxidase/GSH/Mn2+/O2 and malonaldehyde/peroxidase/Mn2+/O2 or by methylene blue (MB) or eosin-sensitized photooxygenation was studied. Our results showed that other ROS were also responsible for XO inactivation when MB was used. In contrast, eosin produced almost exclusively 1O2. Kinetic studies of XO oxidation in the malonaldehyde/peroxidase system showed that histidine (His) is a competitive inhibitor with respect to XO. A similar result was observed in the eosin-photosensitized process, suggesting the involvement of 1O2 in both processes. In addition, an efficient quenching of XO oxidation by guanosine in the folic acid/peroxidase system was observed. Amino acid analysis revealed that cysteine (Cys) is more affected than other XO amino acids also prone to oxidation such as tyrosine (Tyr), methionine (Met) and His. These results indicate that 1O2 may cause oxidative damage to the Cys residues of XO, with loss of enzyme activity. Alteration of the flavin prosthetic site is hypothesized.322145154Floyd, R.A., (1990) FASEB J., 4, pp. 2587-2597Sun, Y., (1990) Free Rad. Biol. 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Physico-chemical characterization of the inclusion complex between a 2-propen-1-amine derivative and beta-cyclodextrin

Inclusion complexes and physical mixtures were prepared with isomeric mixture of E/Z (50:50) of 3-(4'-bromo-[1,1'-biphenyl)-4-yl)-3-(4-bromophenyl)-N,N-dimethyl-2-propen-1-amine (BBAP) and beta-cyclodextrin (beta-CD) in different proportions. In this study, theoretical calculations using Molecular Mechanics MM+ force field were applied to predict the structures of the inclusion complexes formed by interaction of BBAP and beta-cyclodextrin. Circular dichroism, differential thermal analysis (DTA), X-ray diffraction and (13)C CP/MAS NMR methods were used to characterize the inclusion complexes and provide information about the stoichiometry of the inclusion complexes. The combined spectroscopy techniques indicate the formation of a complex of BBAP/beta-CD in the molar proportion of 1:1 and 1:2 by co-evaporation and no complexation was detected in the physical mixture of the compounds.50359159

Violacein/β-cyclodextrin Inclusion Complex Formation Studied By Measurements Of Diffusion Coefficient And Circular Dichroism

The formation of inclusion compounds between violacein and β-cyclodextrin was studied by diffusion and circular dichroism measurements. The present work was undertaken to explore the feasibility of the β-cyclodextrin in reducing the toxicity and enhancing the antitumoral efficacy of violacein by forming an inclusion complex. The results of the two experiments are in good agreement, suggesting the formation of 1 : 1 and 1 : 2 complexes. The diffusion coefficient measurements enabled estimates of the sizes of the complexes involved. From the circular dichroism and computational calculations it was possible to view a preference for inclusion of the most polar part of the molecule to form a 1 : 2 inclusion complex. We expect that this work proves the potential of these techniques to determining complex stoichiometry.3701/04/156774Bortolus, P., Monti, S., (1996) Advances in Photochemistry, 21, p. 1. , D. C. Neckers, D. H. Volman and G. von Bün Wiley-Interscience, New YorkLipkowitz, K.B., (1998) Chem. Rev., 98, p. 1829Dekharsky, M.V., Inoue, Y., (1998) Chem. Rev., 98, p. 1875Saenger, W., (1980) Angew. Chem. Int. Ed. Engl., 19, p. 344Parker, D., Kataky, R., (1997) J. Chem. Soc., Chem. Commun., 2, p. 141Connors, K.A., (1997) Chem. Rev., 97, p. 1325Stella, V.J., Rajewski, R.A., (1997) Pharm. Res., 14, p. 556Koehler, G., Grabner, G., Klein, C.T.H., Marconi, G., Mayer, B., Monti, S., Rechthaler, K., Wolschann, P., (1996) J. Incl. Phenom. Mol. Recognit. Chem., 25, p. 103Beezer, A.E., Mitchell, J.C., (1992) Andrews: Pestic. Sci., 35, p. 375Loh, W., Beezer, A.E., Mitchell, J.C., (1994) Lagmuir, 10, p. 3431Lino, A.C.S., Loh, W., J. Incl. Phenom. Mol. Recognit. Chem., p. 1998. , submittedCohen, A.G.Y., (1997) J. Org. Chem., 62, p. 120Li, M.-X., Li, N.-Q., Gu, Z.-N., Zhou, N.-H., Sun, Y.-L., Wu, Y.-Q., (1996) Electrochim. Acta., 41, p. 2877Manzanares, M.I., Solis, V., De Rossi, R.H., (1996) J. Electroanal. Chem., 407, p. 141Uekama, K., Otagiri, M., Kanie, Y., Tanaka, S., Ikeda, K., (1975) Chem. Pharm. Bull., 23, p. 1421Nakahara, H., Tanaka, H., Kukuda, K., Matsumoto, M., Tagaki, W., (1990) Thin Solid Films, p. 284Guo, R., Chang, J., Lin, S., Chen, R., Hu, J., Zhang, H., (1996) Guangpuxue Yu Guangpu Fenxi., 16, p. 38(1994) Chem. Abstr., 125, p. 86074Hamai, S., (1997) J. Incl. Phenom. Mol. Recognit. Chem., 27, p. 57Mayer, B., Marconi, G., Klein, C., Köhler, G., Wolschann, P., (1997) J. Incl. Phenom. Mol. Recognit. Chem., 29, p. 79Marconi, G., Mayer, B., (1997) Pure Appl. Chem., 69, p. 779Wu, Y., Jin, J., (1966) Sichuan Daxue Xuebao, Ziran Kexueban., 33, p. 560(1997) Chem. Abstr., 126, p. 317579Shen, X., Belletête, M., Durocher, G., (1998) J. Phys. Chem. B, 102, p. 1877Harada, A., Lin, J., Kamachi, M., (1992) Nature, 356, p. 325Harada, A., Lin, J., Kamachi, M., (1994) Nature, 370, p. 126Durán, N., Faljoni-Alario, A., (1980) An. Acad. Brasil. Ciên., 52, p. 287Rettori, D., Durán, N., (1998) World J. Microbiol. Biotechnol., 14, p. 685Haun, M., Pereira, M.F., Hoffmann, M.E., Riveros, R., Joyas, A., Campos, V., Durán, N., (1992) Biol. Res., 25, p. 21Durán, N., Antônio, R.V., Haun, M., Pilli, R.A., (1994) World J. Microbiol. Biotechnol., 10, p. 686Durán, N., Erazo, S., Campos, V., (1983) An. Acad. Brasil. Ciênc., 55, p. 231(1984) Chem. Abstr., 100, pp. 48417bDurán, N., Melo, P.S., Haun, M., (1996) Proc. XXV Annual Meeting Brazilian Biochemical Society, p. 150. , (Escritorio & Editorial, São Paulo, S.P., Brazil), Caxambu, M.G., Brazil O-24Durán, N., Melo, P.S., Haun, M., Proc. VIII Brazilian National Meeting in Virology, p. 1996. , (Brazilian Soc. Virology Publ., UNESP, Jaboticabal, S. P., Brazil), São Lourenço, M.G., BrazilMelo, P.S., Haun, M., Durán, N., (1997) FASEB J., 11 (SUPPL.), pp. A1418Durán, N., Haun, M., Brazilian Patent PI 9702918 (1997)Singh, U.V., Udupa, N., (1997) Indian J. Physiol. Pharmacol., 41, p. 171Singh, U.V., Udupa, N., (1997) Pharm. Sci., 3, p. 573Loh, W., Tonegutti, C.A., Volpe, P.L.O., (1993) J. Chem. Soc. Faraday Trans., 89, p. 113Akizadeth, A., Nieto De Castro, C.A., Wakeham, W.A., (1980) Int. J. Thermophys., 1, p. 243Price, W.E., Trickett, R.A., Harris, K.R., (1989) J. Chem. Soc. Faraday Trans. 1, 85, p. 3281Eastel, A.E., Woolf, L.A., (1989) J. Chem. Soc. Faraday Trans. 1, 80, p. 1287Noulty, R.A., Leaist, D.G., (1987) J. Chem. Eng. Data, 32, p. 418Grabner, G., Monti, S., Marconi, G., Mayer, B., Klein, C., Köhler, G., (1996) J. Phys. Chem., 100, p. 2006

Violacein/beta-cyclodextrin inclusion complex formation studied by measurements of diffusion coefficient and circular dichroism

The formation of inclusion compounds between violacein and beta-cyclodextrin was studied by diffusion and circular dichroism measurements. The present work was undertaken to explore the feasibility of the beta-cyclodextrin in reducing the toxicity and enhancing the antitumoral efficacy of violacein by forming an inclusion complex. The results of the two experiments are in good agreement, suggesting the formation of 1 : 1 and 1 : 2 complexes. The diffusion coefficient measurements enabled estimates of the sizes of the complexes involved. From the circular dichroism and computational calculations it was possible to view a preference for inclusion of the most polar part of the molecule to form a 1 : 2 inclusion complex. We expect that this work proves the potential of these techniques to determining complex stoichiometry.3741730677

Liposome Effect On The Cytochrome C-catalyzed Peroxidation Of Carbonyl Substrates To Triplet Species.

Cytochrome c exhibits peroxidase activity on diphenylacetaldehyde (DPAA) and 3-methylacetoacetone (MAA), which is greatly affected by the presence and nature of charged liposome or micelle interfaces interacting with the enzyme. The ferricytochrome c reaction with DPAA is accelerated when the enzyme is attached to negatively charged interfaces. Whatever the medium, bulk solution or negatively charged dicetylphosphate (DCP), phosphatidylcholine/phosphatidylethanolamine/cardiolipin (PC/PE/CL) liposomes, this chemiluminescent reaction is accompanied by reduction of cytochrome c to its ferrous form. In turn, MAA is oxidized by cytochrome c exclusively when bound to DCP liposomes. Contrary to DPAA oxidation, the MAA reaction is followed by bleaching of cytochrome c, reflecting damage to the hemeprotein chromophore. The cytochrome-c-catalyzed oxidation of either DPAA or MAA leads to concomitant disappearance of the enzyme charge transfer absorption band at 695 nm. This suggests that the peroxidase activity of cytochrome c involves substrate-induced loss of the methionine ligand at the iron sixth coordination position, which is favored by interaction of cytochrome c with negatively charged interfaces. Accordingly, a decrease and blue shift of the charge transfer band could be observed in cytochrome-c-containing negatively charged DCP, PC/PE/CL liposomes or lysophosphatidylethanolamine micelles in the presence of DPAA or MAA.25546-5