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Journal articles on the topic 'Exchange reactions thiol'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Folikumah, Makafui Y., Marc Behl, and Andreas Lendlein. "Reaction behaviour of peptide-based single thiol-thioesters exchange reaction substrate in the presence of externally added thiols." MRS Communications 11, no. 4 (2021): 402–10. http://dx.doi.org/10.1557/s43579-021-00041-z.

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Abstract Identification of patterns in chemical reaction pathways aids in the effective design of molecules for specific applications. Here, we report on model reactions with a water-soluble single thiol-thioester exchange (TTE) reaction substrate, which was designed taking in view biological and medical applications. This substrate consists of the thio-depsipeptide, Ac-Pro-Leu-Gly-SLeu-Leu-Gly-NEtSH (TDP) and does not yield foul-smelling thiol exchange products when compared with aromatic thiol containing single TTE substrates. TDP generates an α,ω-dithiol crosslinker in situ in a ‘pseudo int

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2

Nakagawa, T., E. Aoyama, N. Kobayashi, et al. "Thiol exchange reactions involving selenotrisulfides." Biochemical and Biophysical Research Communications 150, no. 3 (1988): 1149–54. http://dx.doi.org/10.1016/0006-291x(88)90749-8.

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3

Hondal, Robert J., Stefano M. Marino, and Vadim N. Gladyshev. "Selenocysteine in Thiol/Disulfide-Like Exchange Reactions." Antioxidants & Redox Signaling 18, no. 13 (2013): 1675–89. http://dx.doi.org/10.1089/ars.2012.5013.

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4

Yiamsawas, Doungporn, Manfred Wagner, Grit Baier, Katharina Landfester, and Frederik R. Wurm. "Competing and simultaneous click reactions at the interface and in solution." RSC Advances 6, no. 56 (2016): 51327–31. http://dx.doi.org/10.1039/c6ra08880e.

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Two competing click reactions are studied in solution and at the interface of nanodroplets. By adjusting the reaction kinetics, both polyaddition (thiol–maleimide) and polycondensation (disulfide exchange) proceed simultaneously.

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5

Liem-Nguyen, Van, Ulf Skyllberg, Kwangho Nam, and Erik Björn. "Thermodynamic stability of mercury(II) complexes formed with environmentally relevant low-molecular-mass thiols studied by competing ligand exchange and density functional theory." Environmental Chemistry 14, no. 4 (2017): 243. http://dx.doi.org/10.1071/en17062.

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Environmental contextThe chemical speciation of mercury (Hg) largely controls its biogeochemical cycling and exposure to biota. Here, we investigate the thermodynamic stabilities of complexes formed between inorganic divalent Hg (HgII) and 15 biogeochemically relevant low-molecular-mass (LMM) thiol ligands. This information is critical for accurate modelling of the chemical speciation of HgII and to clarify the role of HgII–LMM thiol complexes in the cycling of Hg in the environment. AbstractInorganic divalent mercury (HgII) has a very high affinity for reduced sulfur functional groups. Report

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6

Wang, Chen, Trevor M. Goldman, Brady T. Worrell, Matthew K. McBride, Marvin D. Alim, and Christopher N. Bowman. "Recyclable and repolymerizable thiol–X photopolymers." Materials Horizons 5, no. 6 (2018): 1042–46. http://dx.doi.org/10.1039/c8mh00724a.

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7

Durand, Kirt L., Xiaoxiao Ma, and Yu Xia. "Intra-molecular reactions as a new approach to investigate bio-radical reactivity: a case study of cysteine sulfinyl radicals." Analyst 139, no. 6 (2014): 1327–30. http://dx.doi.org/10.1039/c3an02307a.

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8

Weaver, Kim H., and Dallas L. Rabenstein. "Thiol/Disulfide Exchange Reactions of Ovothiol A with Glutathione." Journal of Organic Chemistry 60, no. 6 (1995): 1904–7. http://dx.doi.org/10.1021/jo00111a065.

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9

Yi, Michael C., and Chaitan Khosla. "Thiol–Disulfide Exchange Reactions in the Mammalian Extracellular Environment." Annual Review of Chemical and Biomolecular Engineering 7, no. 1 (2016): 197–222. http://dx.doi.org/10.1146/annurev-chembioeng-080615-033553.

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10

Pepels, Mark, Ivo Filot, Bert Klumperman, and Han Goossens. "Self-healing systems based on disulfide–thiol exchange reactions." Polymer Chemistry 4, no. 18 (2013): 4955. http://dx.doi.org/10.1039/c3py00087g.

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11

Summa, Domenico, Ottavia Spiga, Andrea Bernini, et al. "Protein-thiol substitution or protein dethiolation by thiol/disulfide exchange reactions: The albumin model." Proteins: Structure, Function, and Bioinformatics 69, no. 2 (2007): 369–78. http://dx.doi.org/10.1002/prot.21532.

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12

Fagan, T. F., and S. G. Mayhew. "Effects of thiols and mercurials on the periplasmic hydrogenase from Desulfovibrio vulgaris (Hildenborough)." Biochemical Journal 293, no. 1 (1993): 237–41. http://dx.doi.org/10.1042/bj2930237.

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The H2-oxidation, H2-production and H-3H-exchange activities of the periplasmic hydrogenase from Desulfovibrio vulgaris (Hildenborough) were almost completely abolished by Hg(II) and the organic mercurials p-chloromercuribenzoate (pCMB) and p-hydroxymercuriphenylsulphonate. The thiol-modifying reagents N-ethylmaleimide, iodoacetate, dithionitrobenzoate and 2-nitro-5-thiocyanobenzoate had no effect on the activities. Kinetic and spectroscopic measurements suggest that inactivation by pCMB involves at least two reactions; a rapid reaction that is reversed by thiols, and a second, slower and irre

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13

Li, Yuzhan, Yuehong Zhang, Orlando Rios, Jong K. Keum, and Michael R. Kessler. "Photo-responsive liquid crystalline epoxy networks with exchangeable disulfide bonds." RSC Advances 7, no. 59 (2017): 37248–54. http://dx.doi.org/10.1039/c7ra06343a.

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14

Netto, Luis Eduardo S., Marcos Antonio de Oliveira, Carlos A. Tairum, and José Freire da Silva Neto. "Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions." Free Radical Research 50, no. 2 (2016): 206–45. http://dx.doi.org/10.3109/10715762.2015.1120864.

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15

Folikumah, Makafui Y., Marc Behl, and Andreas Lendlein. "Thiol–Thioester Exchange Reactions in Precursors Enable pH-Triggered Hydrogel Formation." Biomacromolecules 22, no. 5 (2021): 1875–84. http://dx.doi.org/10.1021/acs.biomac.0c01690.

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16

Theriault, Yvon, and Dallas L. Rabenstein. "A nuclear magnetic resonance study of the equilibria and kinetics of the reaction of penicillamine with cystine and related disulfides." Canadian Journal of Chemistry 63, no. 8 (1985): 2225–31. http://dx.doi.org/10.1139/v85-366.

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The thiol/disulfide exchange reactions of penicillamine (PSH) with cystine and several related disulfides (RSSR) have been studied by 1H nmr. The reactions take place in two steps:[Formula: see text]The equilibria and kinetics of the reactions of PSH with cystine were characterized over the pH range 5–8, while the reactions with the disulfides of cysteamine, homocysteine, 2-mercaptoethanol, mercaptoacetic acid, 3-mercaptopropionic acid, and mercaptosuccinic acid were studied at neutral pH. From the pH dependence of the rate of the reaction of PSH with cystine, the reactive species are identifi

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17

Oka, Ojore B. V., Hui Y. Yeoh, and Neil J. Bulleid. "Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme." Biochemical Journal 469, no. 2 (2015): 279–88. http://dx.doi.org/10.1042/bj20141423.

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The PDI family form disulfide bridges in substrates via thiol-disulfide exchange reactions. We show in the present study that disulfide exchange can occur directly between individual PDI proteins. Implication is that only certain members need to be oxidized or reduced to maintain function.

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18

Jänsch, André, Maher Korakli, Rudi F. Vogel, and Michael G. Gänzle. "Glutathione Reductase from Lactobacillus sanfranciscensis DSM20451T: Contribution to Oxygen Tolerance and Thiol Exchange Reactions in Wheat Sourdoughs." Applied and Environmental Microbiology 73, no. 14 (2007): 4469–76. http://dx.doi.org/10.1128/aem.02322-06.

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ABSTRACT The effect of the glutathione reductase (GshR) activity of Lactobacillus sanfranciscensis DSM20451T on the thiol levels in fermented sourdoughs was determined, and the oxygen tolerance of the strain was also determined. The gshR gene coding for a putative GshR was sequenced and inactivated by single-crossover integration to yield strain L. sanfranciscensis DSM20451TΔgshR. The gene disruption was verified by sequencing the truncated gshR and surrounding regions on the chromosome. The gshR activity of L. sanfranciscensis DSM20451TΔgshR was strongly reduced compared to that of the wild-t

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19

Chabinyc, Michael L., J. Christopher Love, Joseph H. Thywissen, Federico Cervelli, Mara G. Prentiss, and George M. Whitesides. "Self-Assembled Monolayers Exposed to Metastable Argon Beams Undergo Thiol Exchange Reactions." Langmuir 19, no. 6 (2003): 2201–5. http://dx.doi.org/10.1021/la026495i.

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20

Thomas, Sara Anne, Tiezheng Tong, and Jean-François Gaillard. "Hg(ii) bacterial biouptake: the role of anthropogenic and biogenic ligands present in solution and spectroscopic evidence of ligand exchange reactions at the cell surface." Metallomics 6, no. 12 (2014): 2213–22. http://dx.doi.org/10.1039/c4mt00172a.

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21

Woehrle, Gerd H., Leif O. Brown, and James E. Hutchison. "Thiol-Functionalized, 1.5-nm Gold Nanoparticles through Ligand Exchange Reactions: Scope and Mechanism of Ligand Exchange." Journal of the American Chemical Society 127, no. 7 (2005): 2172–83. http://dx.doi.org/10.1021/ja0457718.

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22

Jeong, Dong-Cheol, Bohyun Mun, Hyekyung Lee, et al. "Binaphthyl-based molecular barrier materials for phosphoric acid poisoning in high-temperature proton exchange membrane fuel cells." RSC Advances 6, no. 65 (2016): 60749–55. http://dx.doi.org/10.1039/c6ra13123a.

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23

Rossegger, Elisabeth, Khadijeh Moazzen, Mathias Fleisch, and Sandra Schlögl. "Locally controlling dynamic exchange reactions in 3D printed thiol-acrylate vitrimers using dual-wavelength digital light processing." Polymer Chemistry 12, no. 21 (2021): 3077–83. http://dx.doi.org/10.1039/d1py00427a.

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24

Sousa, Sérgio F., Rui P. P. Neves, Sodiq O. Waheed, Pedro A. Fernandes, and Maria João Ramos. "Structural and mechanistic aspects of S-S bonds in the thioredoxin-like family of proteins." Biological Chemistry 400, no. 5 (2019): 575–87. http://dx.doi.org/10.1515/hsz-2018-0319.

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Abstract Disulfide bonds play a critical role in a variety of structural and mechanistic processes associated with proteins inside the cells and in the extracellular environment. The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Here, we review the structural and mechanistic determinants behind the thiol-disulfide exchange reactions for the different enzyme types within this family, rationalizing the

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25

Woehrle, Gerd H., Marvin G. Warner, and James E. Hutchison. "Ligand Exchange Reactions Yield Subnanometer, Thiol-Stabilized Gold Particles with Defined Optical Transitions." Journal of Physical Chemistry B 106, no. 39 (2002): 9979–81. http://dx.doi.org/10.1021/jp025943s.

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26

Landino, Lisa M., Tara D. Hagedorn, and Kelly L. Kennett. "Evidence for thiol/disulfide exchange reactions between tubulin and glyceraldehyde-3-phosphate dehydrogenase." Cytoskeleton 71, no. 12 (2014): 707–18. http://dx.doi.org/10.1002/cm.21204.

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27

Rabenstein, Dallas L., and Kim H. Weaver. "Kinetics and Equilibria of the Thiol/Disulfide Exchange Reactions of Somatostatin with Glutathione." Journal of Organic Chemistry 61, no. 21 (1996): 7391–97. http://dx.doi.org/10.1021/jo960917+.

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28

Rabenstein, D. L., and P. L. Yeo. "Thiol/Disulfide Exchange Reactions of Captopril and Penicillamine with Arginine Vasopressin and Oxytocin." Bioorganic Chemistry 23, no. 2 (1995): 109–18. http://dx.doi.org/10.1006/bioo.1995.1009.

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29

Li, Tao, Wei Gao, Jingjing Liang, et al. "Biscysteine-Bearing Peptide Probes To Reveal Extracellular Thiol–Disulfide Exchange Reactions Promoting Cellular Uptake." Analytical Chemistry 89, no. 16 (2017): 8501–8. http://dx.doi.org/10.1021/acs.analchem.7b02084.

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30

Pleasants, Joan C., Wei Guo, and Dallas L. Rabenstein. "A comparative study of the kinetics of selenol/diselenide and thiol/disulfide exchange reactions." Journal of the American Chemical Society 111, no. 17 (1989): 6553–58. http://dx.doi.org/10.1021/ja00199a012.

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31

Tang, Zengchao, Paul Wilson, Kristian Kempe, Hong Chen, and David M. Haddleton. "Reversible Regulation of Thermoresponsive Property of Dithiomaleimide-Containing Copolymers via Sequential Thiol Exchange Reactions." ACS Macro Letters 5, no. 6 (2016): 709–13. http://dx.doi.org/10.1021/acsmacrolett.6b00310.

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32

Gao, Wei, Tao Li, Jinghui Wang, Yibing Zhao, and Chuanliu Wu. "Thioether-Bonded Fluorescent Probes for Deciphering Thiol-Mediated Exchange Reactions on the Cell Surface." Analytical Chemistry 89, no. 1 (2016): 937–44. http://dx.doi.org/10.1021/acs.analchem.6b04096.

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33

Simpson, Carrie A., Brian J. Huffman, Aren E. Gerdon, and David E. Cliffel. "Unexpected Toxicity of Monolayer Protected Gold Clusters Eliminated by PEG-Thiol Place Exchange Reactions." Chemical Research in Toxicology 23, no. 10 (2010): 1608–16. http://dx.doi.org/10.1021/tx100209t.

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34

Sengupta, Shantanu, Charles Wehbe, Alana K. Majors, Michael E. Ketterer, Patricia M. DiBello, and Donald W. Jacobsen. "Relative Roles of Albumin and Ceruloplasmin in the Formation of Homocystine, Homocysteine-Cysteine-mixed Disulfide, and Cystine in Circulation." Journal of Biological Chemistry 276, no. 50 (2001): 46896–904. http://dx.doi.org/10.1074/jbc.m108451200.

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Disulfide forms of homocysteine account for >98% of total homocysteine in plasma from healthy individuals. We recently reported that homocysteine reacts with albumin-Cys34-S–S-cysteine to form homocysteine-cysteine mixed disulfide and albumin-Cys34thiolate anion. The latter then reacts with homocystine or homocysteine-cysteine mixed disulfide to form albumin-bound homocysteine (Sengupta, S., Chen, H., Togawa, T., DiBello, P. M., Majors, A. K., Büdy, B., Ketterer, M. E., and Jacobsen, D. W. (2001)J. Biol. Chem. 276, 30111–30117). We now extend these studies to show that human albumin, but no

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35

Phelan, P., та J. P. Malthouse. "13C-n.m.r. of the cyanylated β-lactoglobulins: evidence that Cys-121 provides the thiol group of β-lactoglobulins A and B". Biochemical Journal 302, № 2 (1994): 511–16. http://dx.doi.org/10.1042/bj3020511.

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The thiol groups of beta-lactoglobulins A and B have been cyanylated using [13C]KCN. The samples of [cyanato-13C]-cyanylated-beta-lactoglobulins A and B which we prepared had signals at 109.7 p.p.m. and 114.4 p.p.m. We conclude that the thiocyanate carbon having a chemical shift of 109.7 p.p.m. is in an apolar environment similar to a cyclohexane solvent, whereas the thiocyanate carbon having a chemical shift of 114.4 p.p.m. is in a polar environment similar to water. The signals with chemical shifts of 109.7 p.p.m. are assigned to the thiocyanate carbons of the native [cyanato-13C]cyanylated-

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36

Matei, Clara, Simona Roxana Georgescu, Ilinca Nicolae, et al. "Variations of Thiol–Disulfide Homeostasis Parameters after Treatment with H1-Antihistamines in Patients with Chronic Spontaneous Urticaria." Journal of Clinical Medicine 10, no. 13 (2021): 2980. http://dx.doi.org/10.3390/jcm10132980.

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Background. The pathogenesis of chronic spontaneous urticaria involves metabolic, immunological, and psychological factors. The thiol–disulfide exchange reactions could be a mechanism to counteract oxidative stress in patients with chronic spontaneous urticaria. Objective: The assessment of thiol–disulfide homeostasis parameters (TDHPs) according to disease severity and the influence of H1-antihistamine therapy in patients with chronic spontaneous urticaria. Material and method. We have included 30 patients with chronic spontaneous urticaria in the study and we have determined the levels of na

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37

Zhao, Zichen, Renjie Li, Mahesha M. Poojary, Søren B. Nielsen та Marianne N. Lund. "Effect of Addition of Tryptophan on Aggregation of Apo-α-Lactalbumin Induced by UV-Light". Foods 10, № 7 (2021): 1577. http://dx.doi.org/10.3390/foods10071577.

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UV-B illumination facilitates aggregation of alpha-lactalbumin (α-LA) by intramolecular disulfide bond cleavage followed by intermolecular thiol-disulfide exchange reactions. However, long term exposure to UV-B illumination may induce undesired oxidative modifications of amino acid residues in the protein. The purpose of this study was to examine the effect of UV-induced aggregation of apo-α-LA (a calcium-depleted form of α-LA) under aerobic and anaerobic conditions and by addition of tryptophan (Trp) as a photosensitizer. The addition of Trp to apo-α-LA illuminated under anaerobic conditions

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38

Tovar, Luis E. Rojas, and Michael G. Gänzle. "Degradation of Wheat Germ Agglutinin during Sourdough Fermentation." Foods 10, no. 2 (2021): 340. http://dx.doi.org/10.3390/foods10020340.

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Non Celiac Wheat Sensitivity (NCWS) is an intolerance to wheat products and individuals with NCWS often adhere to a gluten free diet. However, gluten free diets are often associated with a reduced sensory and nutritional quality. Wheat Germ Agglutinin (WGA) is one of the wheat components linked to NCWS. This study explored the fate of WGA during sourdough fermentation. To assess the role of thiol-exchange reactions and proteolysis, sourdoughs were fermented with Fructilactobacillus sanfranciscensis DSM20451, F. sanfranciscensis DSM20451ΔgshR, which lacks glutathione reductase activity, or Lati

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39

Willenbrock, F., and K. Brocklehurst. "Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and a rapid spectroscopic titration of cathepsin H at pH 3-4." Biochemical Journal 227, no. 2 (1985): 511–19. http://dx.doi.org/10.1042/bj2270511.

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A procedure for the isolation of cathepsin B (EC 3.4.22.1) and of cathepsin H from bovine spleen involving covalent chromatography by thiol-disulphide interchange and ion-exchange chromatography was devised. The stabilities of both cathepsins in alkaline media are markedly temperature-dependent, and reliable kinetic data can be obtained at pH values up to 8 by working at 25 degrees C with a continuous spectrophotometric assay. Both enzyme preparations contain only one type of thiol group as judged by reactivity characteristics towards 2,2′-dipyridyl disulphide at pH values up to 8; in each cas

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40

Yazawa, Kenjiro, Hiroyuki Furusawa, and Yoshio Okahata. "Mechanism of Thiol–Disulfide Exchange Reactions between DsbA and DsbB over a Wide pH Range." Chemistry Letters 42, no. 3 (2013): 241–43. http://dx.doi.org/10.1246/cl.2013.241.

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41

Beckmann, Lennart, Christina Charlotte Rolling, Minna Voigtländer, et al. "Bacitracin and Rutin Regulate Tissue Factor Production in Inflammatory Monocytes and Acute Myeloid Leukemia Blasts." Cancers 13, no. 16 (2021): 3941. http://dx.doi.org/10.3390/cancers13163941.

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Aberrant expression of tissue factor (TF) by transformed myeloblasts and inflammatory monocytes drives coagulation activation in acute myeloid leukemia (AML). Although regulation of TF procoagulant activity (PCA) involves thiol-disulfide exchange reactions, the specific role of protein disulfide isomerase (PDI) and other thiol isomerases in AML-associated TF biology is unclear. THP1 cells and peripheral blood mononuclear cells (PBMCs) from healthy controls or AML patients were analyzed for thiol isomerase-dependent TF production under various experimental conditions. Total cellular and membran

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42

Hudson, Devin A., Shawn A. Gannon, and Colin Thorpe. "Oxidative protein folding: From thiol–disulfide exchange reactions to the redox poise of the endoplasmic reticulum." Free Radical Biology and Medicine 80 (March 2015): 171–82. http://dx.doi.org/10.1016/j.freeradbiomed.2014.07.037.

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43

Rottensteiner, Hanspeter, Susanna Skalicky, Birgit Seyfried, et al. "Non-Proteolytic Regulation of the Multimerization of Von Willebrand Factor By ADAMTS13 Based on a Novel Cysteine Thiol Redundancy." Blood 126, no. 23 (2015): 2236. http://dx.doi.org/10.1182/blood.v126.23.2236.2236.

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Abstract The platelet dependent-clotting process is a highly complex pathway that needs to be tightly controlled by a variety of soluble and cellular components. Failure to regulate the activity of multimeric von Willebrand factor (VWF) by ADAMTS13 for instance causes thrombotic thrombocytopenia purpura (TTP). Regulation is achieved through the established function of ADAMTS13 as a VWF-cleaving protease; however, it has been reported that ADAMTS13 may additionally curtail VWF multimer fibrillation by forming disulfide bridges with VWF. Since the latter mechanism remained ill-defined, we aimed

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44

Fila, Karolina, Beata Podkościelna, and Maciej Podgórski. "Cross-Linked Polythiomethacrylate Esters Based on Naphthalene—Synthesis, Properties and Reprocessing." Materials 13, no. 13 (2020): 3021. http://dx.doi.org/10.3390/ma13133021.

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Two structurally different aromatic dithioesters were synthesized from two dithiols and methacryloyl chloride. The polymer networks based on methyl methacrylate and/or styrene and the new dimethacrylates were subsequently prepared. The polymerization yields of copolymers were in the range of 95–99%. The thermal and mechanical properties of the copolymers were determined by means of differential scanning calorimetry (DSC), thermogravimetric analysis (TG/DTG), and Shore D hardness. The addition of dithioesters—1,5-NAF-S-Met (or 1,4(1,5)-NAF-CH2S-Met) (from 0.5% to 5%) to MMA- or ST-based polymer

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45

Bocedi, Alessio, Giada Cattani, Lorenzo Stella, Renato Massoud, and Giorgio Ricci. "Thiol disulfide exchange reactions in human serum albumin: the apparent paradox of the redox transitions of Cys34." FEBS Journal 285, no. 17 (2018): 3225–37. http://dx.doi.org/10.1111/febs.14609.

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46

Sarma, Bani Kanta, and G. Mugesh. "Glutathione Peroxidase (GPx)-like Antioxidant Activity of the Organoselenium Drug Ebselen: Unexpected Complications with Thiol Exchange Reactions." Journal of the American Chemical Society 127, no. 32 (2005): 11477–85. http://dx.doi.org/10.1021/ja052794t.

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47

Chiodo, Fabrizio, Marco Marradi, Javier Calvo, Eloisa Yuste, and Soledad Penadés. "Glycosystems in nanotechnology: Gold glyconanoparticles as carrier for anti-HIV prodrugs." Beilstein Journal of Organic Chemistry 10 (June 12, 2014): 1339–46. http://dx.doi.org/10.3762/bjoc.10.136.

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The therapeutic approach for the treatment of HIV infection is based on the highly active antiretroviral therapy (HAART), a cocktail of antiretroviral drugs. Notwithstanding HAART has shown different drawbacks like toxic side effects and the emergence of viral multidrug resistance. Nanotechnology offers new tools to improve HIV drug treatment and prevention. In this scenario, gold nanoparticles are an interesting chemical tool to design and prepare smart and efficient drug-delivery systems. Here we describe the preparation and antiviral activity of carbohydrate-coated gold nanoparticles loaded

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48

Ahrika, A., M. Anouti, J. E. Robert, and J. L. Paris. "Article." Canadian Journal of Chemistry 76, no. 12 (1998): 1867–74. http://dx.doi.org/10.1139/v98-197.

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S-Aryl thiol esters RC(O)SAr and ArS2- ions are the end products resulting from the reactions between bis(2-nitrophenyl) disulfide Ar2S2 and thiocarboxylate ions RC(O)S- (R = Me, Ph) at 20°C. The apparent SNAr process in fact occurs in two steps as shown by UV-vis absorption spectrophotometry coupled with voltammetry: (i) formation of diacyl disulfides [RC(O)]2S2 and ArS- ions by redox exchange; (ii) subsequent nucleophilic substitution of 2-nitrophenyl thiolate ions at the carbonyl carbon of diacyl disulfides.Key words: diacyl disulfides, 2-nitrophenyldisulfide ions, N,N-dimethylacetamide, nu

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49

Tan, Khoon-Sin, Alan P. Arnold, and Dallas L. Rabenstein. "Selenium-77 nuclear magnetic resonance studies of selenols, diselenides, and selenenyl sulfides." Canadian Journal of Chemistry 66, no. 1 (1988): 54–60. http://dx.doi.org/10.1139/v88-008.

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77Se and 1H nuclear magnetic resonance spectra have been measured for selenols (RSeH), diselenides (RSeSeR), and selenenyl sulfides (RSeSR′), including selenenyl sulfides formed by reaction of glutathione and penicillamine with selenocystine and related diselenides. Exchange processes strongly affect the 77Se and 1H nuclear magnetic resonance spectra of all three classes of compounds. Sharp, exchange-averaged resonances are observed in the 1H nuclear magnetic resonance spectra of selenols; however, selenol proton exchange causes the 77Se resonances to be extremely broad over the pH range where

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Baines, B. S., K. Brocklehurst, P. R. Carey, M. Jarvis, E. Salih, and A. C. Storer. "Chymopapain A. Purification and investigation by covalent chromatography and characterization by two-protonic-state reactivity-probe kinetics, steady-state kinetics and resonance Raman spectroscopy of some dithioacyl derivatives." Biochemical Journal 233, no. 1 (1986): 119–29. http://dx.doi.org/10.1042/bj2330119.

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Abstract:

Chymopapain A was isolated from the dried latex of papaya (Carica papaya) by ion-exchange chromatography followed by covalent chromatography by thiol-disulphide interchange. The latter procedure was used to produce fully active enzyme containing one essential thiol group per molecule of protein, to establish that the chymopapain A molecule contains, in addition, one non-essential thiol group per molecule and to recalculate the literature value of epsilon 280 for the enzyme as 36 000 M−1 × cm −1. The Michaelis parameters for the hydrolysis of L-benzoylarginine p-nitroanilide and of benzyloxy-ca

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