Are Hydrogen Peroxide, Hypochlorite and Peracetic Acid Potential Endocrine Disruptors?

Arylsulfatase and β-glucuronidase are two important enzymes in human, which play important role on dynamic equilibrium of steroidal estrogens. This work probably for the first time reported that hydrogen peroxide (H2O2), hypochlorite and peracetic acid (PAA) could effectively inhibit the activities of arylsulfatase and/or β-glucuronidase. The 50 percent of inhibitions (IC50) of H2O2, and PAA on arylsulfatase were found to be 142.90±9.00, 91.83±10.01, and 43.46±2.92 μM, respectively. The corresponding respective IC50 of hypochlorite and PAA on β-glucuronidase were 704.90±41.40 and 23.26±0.82 μM, while H2O2 showed no inhibition on β-glucuronidase. It was further revealed that the inhibition of hypochlorite on both arylsulfatase and β-glucuronidase was irreversible. On the contrary, the inhibition by H2O2 and PAA was reversible. Moreover, it was found that the inhibitions of arylsulfatase and/or β-glucuronidase by these three chemicals were pH-dependent, among which the inhibition by H2O2 was competitive and non-competitive for PAA. In general, H2O2 and hypochlorite can be endogenously produced in human, which suggested that the two compounds are potential endocrine disruption compounds (EDCs) as they can cause endocrine disruption via inhibition of arylsulfatase and β-glucuronidase. This work further indicated that any agent that can induce production of H2O2 or hypochlorite in human is potential EDC, which explains why some EDCs with very weak or no estrogenic potency can cause endocrine disruption that confirmed in epidemiological studies.

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A Comparative Study on Reactions of Hydrogen Peroxide and Peracetic Acid with Lignin Chromophores. Part 2. The Reaction of Stilbene-Type Model Compounds

Holzforschung ◽

10.1515/hf.2000.026 ◽

2000 ◽

Vol 54 (2) ◽

pp. 153-158 ◽

Cited By ~ 4

Author(s):

George X. Pan ◽

Liam Spencer ◽

Gordon J. Leary

Keyword(s):

Hydrogen Peroxide ◽

Comparative Study ◽

Peracetic Acid ◽

Type Model ◽

Model Compounds ◽

Ph Dependent

Summary The reactions of three hydroxy- and/or methoxy-substituted stilbenes with hydrogen peroxide and peracetic acid have been investigated. Overall, the reactivity of stilbenes was greater towards peracetic acid than towards hydrogen peroxide. Among the stilbene model compounds studied, 4-hydroxystilbene (I) was virtually unreactive to hydrogen peroxide, but was oxidized by peracetic acid to a varying extent that was highly pH-dependent. 4,4′-Dihydroxy-3,3′-dimethoxystilbene (II) and 3,5-dimethoxy-4-hydroxystilbene (III) showed a greater reactivity to either hydrogen peroxide or peracetic acid than 4-hydroxystilbene (I).

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Detection of intermediates and isolation of hydroquinone monoacetate in the Dakin oxidation of p-hydroxyacetophenone

Canadian Journal of Chemistry ◽

10.1139/v78-435 ◽

1978 ◽

Vol 56 (20) ◽

pp. 2646-2649 ◽

Cited By ~ 6

Author(s):

Martin B. Hocking ◽

Ming Ko ◽

Trevor A. Smyth

Keyword(s):

Hydrogen Peroxide ◽

Peracetic Acid ◽

Isolation Procedure ◽

Peroxide Oxidation ◽

Aqueous Hydrogen Peroxide ◽

Butyl Hydroperoxide ◽

Tert Butyl ◽

Tert Butyl Hydroperoxide ◽

Hydrogen Peroxide Oxidation ◽

First Time

Oxidation of o-, m-, and p-hydroxyacetophenone with peracetic acid or tert-butyl hydroperoxide, oxidants relatively readily monitored by nmr, failed to generate isolable intermediates though an intermediate was detected for the p-ketone. Attempted oxidation of a number of related ketones under Dakin conditions failed either to react, or to generate a detectable intermediate. However, with delicate adjustment of pH and careful timing of the isolation procedure, hydroquinone monoacetate has for the first time been successfully isolated from an alkaline aqueous hydrogen peroxide oxidation (Dakin oxidation) of p-hydroxyacetophenone.

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Inhibition Properties of Arylsulfatase and β-Glucuronidase by Hydrogen Peroxide, Hypochlorite, and Peracetic Acid

ACS Omega ◽

10.1021/acsomega.0c06060 ◽

2021 ◽

Author(s):

Shu-shu Zhong ◽

Jun Zhang ◽

Ze-hua Liu ◽

Zhi Dang ◽

Yu Liu

Keyword(s):

Hydrogen Peroxide ◽

Peracetic Acid

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Modeling and Molecular Dynamics of the 3D Structure of the HPV16 E7 Protein and Its Variants

International Journal of Molecular Sciences ◽

10.3390/ijms22031400 ◽

2021 ◽

Vol 22 (3) ◽

pp. 1400

Author(s):

Ciresthel Bello-Rios ◽

Sarita Montaño ◽

Olga Lilia Garibay-Cerdenares ◽

Lilian Esmeralda Araujo-Arcos ◽

Marco Antonio Leyva-Vázquez ◽

...

Keyword(s):

Molecular Dynamics ◽

3D Structure ◽

Epidemiological Studies ◽

Dynamics Simulation ◽

Structural Refinement ◽

Oncogenic Potential ◽

Structural Differences ◽

Reference Protein ◽

E6 And E7 ◽

First Time

The oncogenic potential of high-risk human papillomavirus (HPV) is predicated on the production of the E6 and E7 oncoproteins, which are responsible for disrupting the control of the cell cycle. Epidemiological studies have proposed that the presence of the N29S and H51N variants of the HPV16 E7 protein is significantly associated with cervical cancer. It has been suggested that changes in the amino acid sequence of E7 variants may affect the oncoprotein 3D structure; however, this remains uncertain. An analysis of the structural differences of the HPV16 E7 protein and its variants (N29S and H51N) was performed through homology modeling and structural refinement by molecular dynamics simulation. We propose, for the first time, a 3D structure of the E7 reference protein and two of Its variants (N29S and H51N), and conclude that the mutations induced by the variants in N29S and H51N have a significant influence on the 3D structure of the E7 protein of HPV16, which could be related to the oncogenic capacity of this protein.

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Inactivation of Prions by Low-Temperature Sterilization Technology Using Vaporized Gas Derived from a Hydrogen Peroxide–Peracetic Acid Mixture

Pathogens ◽

10.3390/pathogens10010024 ◽

2020 ◽

Vol 10 (1) ◽

pp. 24

Author(s):

Akikazu Sakudo ◽

Daiki Anraku ◽

Tomomasa Itarashiki

Keyword(s):

Hydrogen Peroxide ◽

Medical Devices ◽

Neurodegenerative Disorders ◽

Peracetic Acid ◽

Protein Misfolding ◽

Prion Diseases ◽

Proteinase K ◽

Acid Mixture ◽

Cover Glass ◽

Standard Mode

Prion diseases are proteopathies that cause neurodegenerative disorders in humans and animals. Prion is highly resistant to both chemical and physical inactivation. Here, vaporized gas derived from a hydrogen peroxide–peracetic acid mixture (VHPPA) was evaluated for its ability to inactivate prion using a STERIACE 100 instrument (Saraya Co., Ltd.). Brain homogenates of scrapie (Chandler strain) prion-infected mice were placed on a cover glass, air-dried, sealed in a Tyvek package, and subjected to VHPPA treatment at 50–55 °C using 8% hydrogen peroxide and <10% peracetic acid for 47 min (standard mode, SD) or 30 min (quick mode, QC). Untreated control samples were prepared in the same way but without VHPPA. The resulting samples were treated with proteinase K (PK) to separate PK-resistant prion protein (PrPres), as a marker of the abnormal isoform (PrPSc). Immunoblotting showed that PrPres was reduced by both SD and QC VHPPA treatments. PrPres bands were detected after protein misfolding cyclic amplification of control but not VHPPA-treated samples. In mice injected with prion samples, VHPPA treatment of prion significantly prolonged survival relative to untreated samples, suggesting that it decreases prion infectivity. Taken together, the results show that VHPPA inactivates prions and might be applied to the sterilization of contaminated heat-sensitive medical devices.

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The application of inexpensive and synthetic simple electrocatalyst CuFe-MoC@NG in immunosensor

The Analyst ◽

10.1039/d1an00840d ◽

2021 ◽

Author(s):

Lisha Mei ◽

Wentang Zhao ◽

Yiju Song ◽

Li Zhang ◽

Mengmeng Zhang ◽

...

Keyword(s):

Hydrogen Peroxide ◽

Precious Metal ◽

Doped Graphene ◽

One Step ◽

Metal Materials ◽

First Time

In this study, we used inexpensive and synthetic simple electrocatalysts replacement conventional precious metal materials to reduce hydrogen peroxide (H2O2). We first time developed N-doped graphene-coated CuFe@MoC using one-step calcination...

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Farringtonite as an efficient catalyst for linear-chain α-olefin epoxidation with aqueous hydrogen peroxide

New Journal of Chemistry ◽

10.1039/d1nj01872h ◽

2021 ◽

Author(s):

Xingyu Yang ◽

Xu Li ◽

Jinxiang Dong

Keyword(s):

Hydrogen Peroxide ◽

Transition Metals ◽

Linear Chain ◽

Olefin Epoxidation ◽

Aqueous Hydrogen Peroxide ◽

Efficient Catalyst ◽

First Time

A convenient, scalable, benign, and efficient epoxidation method based on farringtonite, without the use of transition metals, was developed for the first time.

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What induces colitis? Hydrogen peroxide or peracetic acid

Endoscopy ◽

10.1055/s-2007-995417 ◽

2008 ◽

Vol 40 (03) ◽

pp. 231-231 ◽

Cited By ~ 2

Author(s):

R. Coriat ◽

U. Chaput ◽

Z. Ismaili ◽

S. Chaussade

Keyword(s):

Hydrogen Peroxide ◽

Peracetic Acid

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Phosphate-Catalyzed Hydrogen Peroxide Formation from Agar, Gellan, and κ-Carrageenan and Recovery of Microbial Cultivability via Catalase and Pyruvate

Applied and Environmental Microbiology ◽

10.1128/aem.01366-17 ◽

2017 ◽

Vol 83 (21) ◽

Cited By ~ 12

Author(s):

Kosei Kawasaki ◽

Yoichi Kamagata

Keyword(s):

Hydrogen Peroxide ◽

Phosphate Buffer ◽

Laboratory Culture ◽

Colony Count ◽

Natural Environments ◽

Ammonium Ions ◽

Factors Affecting ◽

Culture Techniques ◽

Ph Dependent ◽

Growth Inhibiting

ABSTRACTPreviously, we reported that when agar is autoclaved with phosphate buffer, hydrogen peroxide (H2O2) is formed in the resulting medium (PT medium), and the colony count on the medium inoculated with environmental samples becomes much lower than that on a medium in which agar and phosphate are autoclaved separately (PS medium) (T. Tanaka et al., Appl Environ Microbiol 80:7659–7666, 2014,https://doi.org/10.1128/AEM.02741-14). However, the physicochemical mechanisms underlying this observation remain largely unknown. Here, we determined the factors affecting H2O2formation in agar. The H2O2formation was pH dependent: H2O2was formed at high concentrations in an alkaline or neutral phosphate buffer but not in an acidic buffer. Ammonium ions enhanced H2O2formation, implying the involvement of the Maillard reaction catalyzed by phosphate. We found that other gelling agents (e.g., gellan and κ-carrageenan) also produced H2O2after being autoclaved with phosphate. We then examined the cultivability of microorganisms from a fresh-water sample to test whether catalase and pyruvate, known as H2O2scavengers, are effective in yielding high colony counts. The colony count on PT medium was only 5.7% of that on PS medium. Catalase treatment effectively restored the colony count of PT medium (to 106% of that on PS medium). In contrast, pyruvate was not as effective as catalase: the colony count on sodium pyruvate-supplemented PT medium was 58% of that on PS medium. Given that both catalase and pyruvate can remove H2O2from PT medium, these observations indicate that although H2O2is the main cause of reduced colony count on PT medium, other unknown growth-inhibiting substances that cannot be removed by pyruvate (but can be by catalase) may also be involved.IMPORTANCEThe majority of bacteria in natural environments are recalcitrant to laboratory culture techniques. Previously, we demonstrated that one reason for this is the formation of high H2O2levels in media prepared by autoclaving agar and phosphate buffer together (PT medium). In this study, we investigated the factors affecting H2O2formation from agar. H2O2formation is pH dependent, and ammonium ions promote this phosphate-catalyzed H2O2formation. Amendment of catalase or pyruvate, a well-known H2O2-scavenging agent, effectively eliminated H2O2. Yet results suggest that growth-inhibiting factor(s) that cannot be eliminated by pyruvate (but can be by catalase) are present in PT medium.

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