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3.
J Hazard Mater ; 391: 122225, 2020 06 05.
Artigo em Inglês | MEDLINE | ID: mdl-32062539

RESUMO

This work has assessed the impact of typical heavy metal cations on C-phycocyanin in vitro and in silico. At low concentrations (<2×10-6 mol/L), the influence of Pb2+ is the highest on the light absorption of C-phycocyanin trimer. At higher concentrations, however, a new order of influence on the light absorption has been observed with Cd2+ < Cu2+ < Pb2+ < Zn2+. The fluorescence polarization has changed from the order of Cd2+ < Pb2+≈Cu2+ < Zn2+ to Cd2+ < Cu2+ < Pb2+ < Zn2+, when the metal concentrations reaches 2×10-6 mol/L. The mechanisms for these findings have been studied using FTIR, hydrophobic probe, isothermal titration calorimetry and molecular docking for the analysis of structure disorder of C-phycocyanin. It has been suggested that the secondary structure of C-phycocyanin affects more to the light absorbance while the fluorescence characteristics relies more on the tertiary structure. The interaction between Pb2+ and C-phycocyanin is both enthalpically and entropically favoured, whereas the interactions for Cd2+, Cu2+ and Zn2+ are entropically driven. The ion-molecular docking suggests that the structure disorder of C-phycocyanin relies on the molecular interactions with metal ions. The in silico study also showed that the binding cites of Zn2+ are closer to chromophores.


Assuntos
Metais Pesados/química , Ficocianina/química , Sítios de Ligação , Simulação de Acoplamento Molecular , Fotossíntese , Conformação Proteica
4.
Dose Response ; 17(4): 1559325819891378, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-31819742

RESUMO

The increasing use of ionizing radiation (IR) in medical diagnosis and treatment has caused considerable concern regarding the effects of occupational exposure on human health. Despite this concern, little information is available regarding possible effects and the mechanism behind chronic low-dose irradiation. The present study assessed potential genomic damage in workers occupationally exposed to low-dose X-rays. A variety of analyses were conducted, including assessing the level of DNA damage and chromosomal aberrations (CA) as well as cytokinesis-block micronucleus (CBMN) assay, gene expression profiling, and antioxidant level determination. Here, we report that the level of DNA damage, CA, and CBMN were all significantly increased. Moreover, the gene expression and antioxidant activities were changed in the peripheral blood of men exposed to low-dose X-rays. Collectively, our findings indicated a strong correlation between genomic instability and duration of low-dose IR exposure. Our data also revealed the DNA damage repair and antioxidative mechanisms which could result in the observed genomic instability in health-care workers exposed to chronic low-dose IR.

5.
Environ Sci Pollut Res Int ; 25(32): 32373-32380, 2018 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-30229494

RESUMO

This work reports the toxicity of small silver nanoparticles (nanoAg, 20 nm) and silver ions (Ag+) to the red blood cells with the silver concentration level of 10-6 g/mL. Results show that red blood cells (RBCs) start hemolysis when treated by nanoAg of 1.5 × 10-5 g/mL or Ag+ of 2.9 × 10-7 g/mL. A low ATPase activity of 30% has been observed after RBCs being treated with Ag+ of 2.6 × 10-7 g/mL, while the nanoAg does not obviously affect the ATPase activity. In molecular level, Ag+ is more toxic to the amino acid residues than nanoAg according to the change of fluorescence characteristics of hemoglobin (Hb). However, the nanoAg has been found to be more toxic than Ag+ to the secondary structure of Hb in terms of the loss of α-helix content.


Assuntos
Eritrócitos/efeitos dos fármacos , Hemoglobinas/metabolismo , Hemólise/efeitos dos fármacos , Nanopartículas Metálicas/toxicidade , Prata/toxicidade , Adenosina Trifosfatases/metabolismo , Aminoácidos/metabolismo , Exposição Ambiental , Eritrócitos/metabolismo , Eritrócitos/patologia , Humanos , Íons
6.
Environ Pollut ; 242(Pt B): 1939-1949, 2018 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-30055792

RESUMO

Di-(2-ethylhexyl) phthalate (DEHP) associated in vitro/vivo toxicity at current environmentally relevant concentration (ERC) with attendant ecological risks in the Three Gorges Reservoir Area (TGRA) is still elusive. Responding to this challenge, a novel integrated study based on analytical and biological assays was designed to elucidate the underlying mechanisms for toxicity of DEHP and its ecological risks at ERC. In this study, GC-MS analysis showed that the highest environmental concentration of DEHP in the TGRA surface water was nearly double that of WHO and USEPA standards. Both distribution and ecological risk decreased from the upper to middle and lower reaches of the TGRA. In vitro toxicity was assessed by cell viability and DNA damage assays: DEHP exposure at ERCs (100-800 µg/L) caused significant reduction in cell viability and elevated DNA damage. Further, DEHP exposure above 400 µg/L resulted in enhanced migration behavior of cancer cells. For in vivo toxicity assessment, short term acute exposure (7 d, 400 µg/L) apparently activated the PI3K-AKT-mTOR pathway, and chronic low-level exposure (3 months, 10-33 µg/L) suppressed the hypothalamus pituitary thyroid (HPT) axis pathway in zebrafish. In addition, acute low-level exposure (5 d, 33-400 µg/L) to DEHP increased aryl hydrocarbon receptor (AhR) activity in Tg(cyp1a:gfp) zebrafish in a concentration-dependent manner. In short, DEHP at ERC has extended potential to induce diverse in vitro and in vivo toxicity at concentrations that also cause impairment of biochemical function in aquatic species of the TGRA.


Assuntos
Dietilexilftalato/toxicidade , Poluentes Ambientais/toxicidade , Testes de Toxicidade , Animais , China , Dano ao DNA , Ecologia , Fosfatidilinositol 3-Quinases/metabolismo , Ácidos Ftálicos , Medição de Risco , Serina-Treonina Quinases TOR/metabolismo , Peixe-Zebra/fisiologia
7.
Chemosphere ; 192: 171-177, 2018 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-29101856

RESUMO

This work reports the influence of lead (Pb2+) on fluorescence characteristics and protein structure of phycocyanin molecules experimentally in vitro. The fluorescence intensity decreases with the increasing concentration of Pb2+ from 0 to 5 × 10-5 mol L-1, showing the fluorescence quenching of phycocyanin by Pb2+. The quenching process is suggested to be static regarding the calculation results and the experimental results of time-resolved fluorescence decay profiles. The synchronous fluorescence spectra show that the effect of Pb2+ on the Tyr residues of phycocyanin is more significant than the Trp residues. The forming of aggregation by the interaction of Pb2+ with phycocyanin molecules is suggested from the results of resonance light scattering spectra. The UV-Vis spectra of the protein skeleton of phycocyanin have a red-shift of about 10 nm with increasing the Pb2+ concentration from 0 to 5 × 10-5 mol L-1, indicating a change in the protein skeleton and its secondary structure. With the increasing Pb2+ concentration, the two negative peaks (209 nm and 218 nm) on circular dichroism spectra become smaller, showing a decrease of the α-helix structure. These results may give people a deeper understanding of that how the heavy metal (Pb2+) can affect the chemo-physical properties of phycocyanin.


Assuntos
Chumbo/química , Ficocianina/química , Dicroísmo Circular , Chumbo/toxicidade , Estrutura Secundária de Proteína , Espectrometria de Fluorescência
8.
Chemosphere ; 185: 29-35, 2017 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-28683334

RESUMO

In this work, interactions of three phthalate acid esters (PAEs), including dimethyl phthalate (DMP), diethyl phthalate (DEP) and dibutyl phthalate (DBP), with trypsin have been studied in vitro, under simulated physiological conditions using multi-spectroscopic techniques and molecular modeling. The results show that these PAEs can bind to the trypsin, forming trypsin-PAEs complexes, mainly via hydrophobic interactions, with the affinity order of DMP > DEP > DBP. Binding to the PAEs is found to result in molecular deformation of trypsin. The modeling results suggest that only DBP can bind with the amino acid residues of the catalytic triad and S1 binding pocket of trypsin, leading to potential competitive enzyme inhibition.


Assuntos
Ésteres/química , Modelos Químicos , Ácidos Ftálicos/química , Tripsina/química , Dibutilftalato/química
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