Effect of radioactive and non-radioactive mercury on wheat germination and the anti-toxic role of glutathione

Popa, Karin; Murariu, Manuela; Molnar, R; Schlosser, Gitta; Cecal, Alexandru; Drochioiu, Gabi

doi:10.1080/10256010701362112

Cited by 18 publications

(12 citation statements)

References 24 publications

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“…26 However, cysteine-containing peptides, such as glutathione, have the highest affinity toward heavy metal ions, whereas glycine-rich P19 peptides have a lower one. [37][38][39] our results are concordant with the mechanism previously described, whereby an analog of the human albumin N-terminus (Asp-Ala-His-Lys) prevents formation of copper-induced reactive oxygen species and potentially provide therapeutic benefit for roS-related diseases. 28 A neuroprotective ability was described in the case of tetrapeptide L-Asp-Ala-His-Lys in permanent middle cerebral artery occlusion in rats.…”

Section: Biomedical Implicationssupporting

confidence: 90%

Electrospray Ionization Mass Spectrometric Approach of Conformationally-Induced Metal Binding to Oligopeptides

Murariu¹,

Drăgan²,

Drochioiu

2010

Eur J Mass Spectrom (Chichester)

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Electrospray ionization mass spectrometry was used to measure the binding of copper and nickel ions to the newly synthesized model peptides H(2)N-AAAAHAAAAHAAAAHAAAA-COOH (P19-H5) and H(2)N-AAAHAAAHAAAHAAAAAAA-COOH (P19-H4). The affinity of histidine-containing peptides toward heavy metal ions proved to be related to the position of each histidine residue in the peptide sequence. In contrast to P19-H5, P19-H4 peptide bound no nickel or copper ions in the gas phase, whereas its spectra showed an intense fragmentation. The role of spacing residues (Ala repeats) in selecting the various conformations was also investigated. Finally, the circular dichroism and Fourier transform infrared spectra indicated that these isomer peptides have quite different conformations. A close relationship between the conformation of alanine-based peptides and their affinity toward metal ions may result in different patterns of metal ion-peptide systems.

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Section: Biomedical Implicationssupporting

confidence: 90%

Electrospray Ionization Mass Spectrometric Approach of Conformationally-Induced Metal Binding to Oligopeptides

Murariu¹,

Drăgan²,

Drochioiu

2010

Eur J Mass Spectrom (Chichester)

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“…The previous results demonstrated that potential target sites for the evaluation of metal binding need to be carefully analyzed for interfering metal-metal interactions [19,[23][24][25][26][27][28]. In this study, decreases of bound silver by Aβ, and an increase in bound copper were the most pronounced interactions between the two toxic metals (Figure 3).…”

Section: Metal-metal Interactions During the Binding Processmentioning

confidence: 83%

Interaction of β-amyloid(1-40) peptide with pairs of metal ions: An electrospray ion trap mass spectrometric model study

Drochioiu

Manea

Drăguşanu

et al. 2009

Biophysical Chemistry

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT 2 AbstractThe stoichiometries and the affinity toward simple and paired metal ions of synthetic amyloid-β(1-40)peptide (Aβ1-40) were investigated by electrospray ion trap mass spectrometry (ESI-MS), circular dichroism (CD), and atomic force microscopy (AFM). The results lead to the working hypothesis that pHdependent metal binding to Aβ1-40 may induce conformational changes, which affect the affinity toward other metals. A significant copper and zinc binding to Aβ1-40 peptide at pH 5.5 was found, whereas nickel ions commonly bind to each molecule of β-amyloid peptide. Some complexes of Aβ1-40 with more than one nickel ion were identified by ESI-MS. In addition, nickel ions proved to enhance Aβ oligomerization. On increasing pH, up to 12 ions of zinc may bind to a single Aβ molecule. Under the same pH and concentration conditions, the binding pattern of the independent copper and silver ions to Aβ1-40 was different from that of the equimolecular mixture of the two metal ions. One might assume that some conformational changes due to water loss altered the capacity of Aβ peptide to bind certain heavy metal ions. As a consequence, copper-silver interaction with the binding process to Aβ1-40 became highly complex. A competition between silver and nickel ions for Aβ1-40 binding sites at high pH was also observed. New strategies were proposed to identify the characteristic signals for some important metal ion-peptide complexes in the spectra recorded at high pH or high concentrations of metal ions. To explain the formation of such a large number of high metal ion-Aβ complexes, we took into consideration the participation of both histidine residues and free amino groups as well as carboxylate ones in the binding process. Finally, CD and AFM studies supported the mass spectrometric data.

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“…Mass spectrometric analysis of DNP degradation products revealed the presence of 6-hydroxy-3,5-dinitrohexa-2,4-dienal as the main constituent of the irradiated solution. Moreover, both the infrared spectroscopy and the wheat germination experiment , [14][15][16][17] using the supernatant that contained photodegraded DNP, confirmed the fast disappearance of the toxicity. Besides, Fourier transform-infrared (FT-IR) spectra indicated the formation of a nonaromatic aldehyde.…”

Section: Introductionmentioning

confidence: 90%

Letter: Study on the Mechanism of Ferrite-Induced Dinitrophenol Photodegradation

Zaharia

Borhan

Ghercă

et al. 2014

Eur J Mass Spectrom (Chichester)

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We report here the effectiveness of gas chromatography mass spectrometry techniques in establishing the ferrite-associated photocatalytic degradation mechanism of pesticide 2,4-dinitrophenol (2,6-DNP). Unlike the previously discussed DNP-degradation mechanisms that involve either oxidation or reduction reactions, ferrite-based ultraviolet (UV) photodegradation of DNP affords the nontoxic 6-hydroxy-3,5-dinitrohexa-2,4-dienal by an unusual water addition to the benzene core. We searched for and demonstrated the presence of an epoxide of DNP within the photodegradation process, which may unambiguously explain the novel photochemical mechanism. During the 15 min UV photoinduced process, DNP degradation efficiency on the zinc ferrite catalyst was calculated to be 82%, whereas the first-order kinetic rate constant k was as high as 3.4 x 10(-2)min(-1).

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Effect of radioactive and non-radioactive mercury on wheat germination and the anti-toxic role of glutathione

Cited by 18 publications

References 24 publications

Electrospray Ionization Mass Spectrometric Approach of Conformationally-Induced Metal Binding to Oligopeptides

Electrospray Ionization Mass Spectrometric Approach of Conformationally-Induced Metal Binding to Oligopeptides

Interaction of β-amyloid(1-40) peptide with pairs of metal ions: An electrospray ion trap mass spectrometric model study

Letter: Study on the Mechanism of Ferrite-Induced Dinitrophenol Photodegradation

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