464. The reactions of certain epoxides in aqueous solutions

Ross, W. C. J.

doi:10.1039/jr9500002257

Cited by 156 publications

(67 citation statements)

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“…In contrast, DEB generally reacts via an S N 2 mechanism with attack on the least substituted carbon in concert with ring opening (44,45). The second epoxide ring then reacts readily, leading to relatively fast closure of monoadducts to cross-links (46).…”

Section: Discussionmentioning

confidence: 99%

DNA Interstrand Cross-Linking by Epichlorohydrin

Romano

Newman

Zahran

et al. 2007

Chem. Res. Toxicol.

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Epichlorohydrin (ECH), an important industrial chemical, is a bifunctional alkylating agent with the potential to form DNA cross-links. Occupational exposure to this suspect carcinogen leads to chromosomal aberrations, and ECH has been shown previously to undergo reaction with DNA in vivo and in vitro.We used denaturing polyacrylamide gel electrophoresis to monitor the possible formation of interstrand cross-links within DNA oligomers by ECH and the related compound, epibromohydrin (EBH). Although both compounds did indeed form cross-links between deoxyguanosine residues, EBH was a more efficient cross-linker than ECH. The optimal pH for cross-linking also varied, with ECH more efficient at pH 5.0 and EBH more efficient at pH 7.0. Both agents were relatively flexible in the sequences targeted, with comparable efficiencies for 5′-GGC and 5′GC sites. Furthermore, interstrand cross-linking by the two optical isomers of ECH correlated with their relative cytotoxicities, with R-ECH about twice as potent as S-ECH.

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Section: Discussionmentioning

confidence: 99%

DNA Interstrand Cross-Linking by Epichlorohydrin

Romano

Newman

Zahran

et al. 2007

Chem. Res. Toxicol.

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“…In contrast, treatment with 3 or 5% GLD for 12 hr dramatically reduced the detectable antigenicity of PrP Sc . In addition, GLD is far more easier to handle than LEO and is stable in aqueous solution because its hydrolysis occurs rather slowly (t1/2 at 37°C is 100 hr) [17]. Therefore, GLD is the most potential on prion inactivation among the three epoxides.…”

Section: Discussionmentioning

confidence: 99%

“…GLD is also known to be mutagenic and carcinogenic, however, there are great differences in susceptibility among species [9,10]. For safety, it may be desirable to wash GLD off from the treated materials with weak acid because GLD degrades to glycerol in acidic environment [17].…”

Section: Discussionmentioning

confidence: 99%

“…The results suggest that the influence of salt concentrations differed from pH and the contents of the buffers used but GLD degraded PrP Sc more efficiently at alkaline environment if salt concentrations are unchanged. GLD is known to be reactive with sodium and degrades in acidic pH [17]. These factors need to be considered to optimize the GLD treatment condition.…”

Section: Discussionmentioning

confidence: 99%

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Glycidol Degrades Scrapie Mouse Prion Protein.

Yamamoto

Horiuchi

Ishiguro

et al. 2001

The Journal of Veterinary Medical Science

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ABSTRACT. Agents of transmissible spongiform encephalopathy (prion) are known to be extremely resistant to physicochemical inactivation procedures such as heat, radiation, chemical disinfectants such as detergents, alcohols, glutaraldehyde, formalin, and so on. Because of its remarkable resistance, it is difficult to inactivate prion. Chemical inactivation seems to be a practical method because it is applicable to large or fixed surfaces and complicated equipment. Here, three epoxides: β-propiolactone, propylene oxide, and glycidol (GLD) were examined of their inactivation ability against scrapie-mouse prion protein (PrP Sc ) under various conditions of chemical concentration, incubation time, and temperature. Among these chemicals, GLD worked most effectively and degraded PrP into small fragments. As a result of the bioassay, treatment with 3% GLD for 5 hr and 5% GLD for 2, 5 hr or 12 hr at room temperature prolonged the mean incubation time by 44, 30, 110 and 73 days, respectively. From dose-incubation time standard curve, the decrease in infectivity titers were estimated as 10 3 or more. Therefore, degradation of PrP Sc by GLD decreased the scrapie infectivity. It is also suggested that pH and salt concentrations influence the effect of GLD. Although further study is necessary to determine the optimal condition, GLD may be a potential prion disinfectant.

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“…The value k KR is about 10 5 times larger than the second order rate constant of spontaneous addition of anion to epoxide, 21) also supporting the suicide substrate based inactivation of E5G. The k KR value for E5G inactivation of IMDex was reported to be 1.16 min −1 mM −1 , 18) which is 3.8 times higher than that of SmDex.…”

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confidence: 97%

Suicide Substrate-based Inactivation of Endodextranase by .OMEGA.-Epoxyalkyl .ALPHA.-D-Glucopyranosides

ヒゴン¹,

ヨンミン²,

博之³

et al. 2010

J. Appl. Glycosci.

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Dextranases are enzymes that hydrolyze the α 1,6 glucosyl backbone chain of dextran and isomaltooligosaccharides. Dextranases are classified as endolytic enzymes (endodextranase) or exolytic enzymes (exodextranase) by their reaction modes. Furthermore, dextranases are divided into several families on the basis of the similarity in their amino acid sequences. 1,2) Most endodextranases belong to glycoside hydrolase family (GH) 49 and 66, and exodextranases belong to GH13,15, 27, 49 and 87. 3) The dextranase from Streptococcus mutans ATCC 25175 (SmDex) is an endodextranase (EC 3.2.1.11; 6 α D glucan 6 glucanohydrolase) that is classified under GH66. GH66 enzymes are composed of endodextranase and cycloisomaltooligosaccharide glucanotransferase 4) (EC 2.4.1.248; (1 6) α D glucan:(1 6) α D glucan 6 α D (1 6α D glucano) transferase (cyclizing)). In GH66 members, twenty nine enzymes have been reported and sixteen enzymes have been characterized at present.There are two types of chemical modification reagents based on their inactivation mechanisms, 5) i) two molecules reaction type (Equation (1)) and ii) intermediate formation type (Equation (2)) as follows:where E, R, E R and E R are intact enzyme, chemical modification reagent, inactivated enzyme bound by reagent covalently, and reversible intermediate complex, respectively. In Equation (2), k and KR are the rate constant of irreversible inactivation and dissociation constant of intermediate complex, respectively. Inactivation of the suicide substrate (mechanism based inactivator) follows the intermediate formation type mechanism. 6) Suicide substrate itself is an inert compound that does not attack any free amino acid. When this compound is incorporated into the catalytic site of an enzyme, its inert active species is activated by enzyme reaction to form the covalent linkage with amino acid residue, resulting in the inactivation of the enzyme. 6) Epoxyalkyl based suicide substrate is an effective material to label the catalytic residues and has been applied in a number of glycosidases. 7 17) ω Epoxyalkyl α glucopyranosides have already been reported to show irreversible inhibition to the isomalto dextranase (IMDex) (EC 3.2.1.94; 6 α D glucan isomaltohydrolase) from Arthrobacter globiformis T6 with the suicide substrate mechanism. 18) IMDex is an exodextranase which produces isomaltose from the non reducing terminal of dextran, suggesting a possibility that ω epoxyalkyl α glucopyranoside also becomes a suicide substrate for endodextranase. Therefore, 3 ,4 epoxybutyl α D glucopyranoside (E4G), 4 ,5 epoxypentyl α D glucopyranoside (E5G), and 5 ,6 epoxyhexyl α D J. Appl. Glycosci., 57, 269 272 (2010)

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464. The reactions of certain epoxides in aqueous solutions

Cited by 156 publications

References 0 publications

DNA Interstrand Cross-Linking by Epichlorohydrin

DNA Interstrand Cross-Linking by Epichlorohydrin

Glycidol Degrades Scrapie Mouse Prion Protein.

Suicide Substrate-based Inactivation of Endodextranase by .OMEGA.-Epoxyalkyl .ALPHA.-D-Glucopyranosides

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