J. Chem. Chem. Eng. 9 (2015) 324-328
doi: 10.17265/1934-7375/2015.05.003
Infrared Spectra and X-ray Examination of the Complex Albumin Human with UO22+
Aibassov Yerkin Zhakenovich1*, Yemelyanova Valentina1, Shakieva Tatyana1, Nakisbekov Narymzhan2, Tussupbaev Nessipbay1, Abenov Bakhyt1, Bulenbayev Maxat1, Dossumova Binara1 and Blagikh Evgeniy1
1. Rearch Institute of New Chemical Technologies and Materials, Kazakh National University Al-Farabi, Almaty 005012, Kazakhstan
2. Institute of Fundamental and Applied Medicine, Kazakh National Medical University, Almaty 005012, Kazakhstan
Abstract: Reaction dioxouraniun (VI) UO22+ ion with human rum albumin was prepared: human albumin with uranium UO22+ ion and the X-ray method of investigation of the complexes. The authors have shown that Human Albumin may be ud to remove highly toxic uranyl UO22+ ions.
Key words: Albumin rum human, dioxouraniun (VI) UO22+ ion, X-ray, complex.
塑胶跑道做法
1. Introduction
Human rum albumin is the most abundant protein
in human blood plasma. It is produced in the liver. Albumin constitutes about half of the blood rum protein. It is soluble and monomeric. Albumin transports hormones, fatty acids, and other compounds, buffers pH, and maintains osmotic pressure, among other functions. Albumin is synthesized in the liver as
a prealbumin, which has an N-terminal peptide, which
is removed before the protein is relead from occurring rough endoplasmic reticulum human. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the creted albumin.
The approximate quence of human rum albumin is:
着装得体MKWVTFISLL FLFSSAYSRG VFRR DAHKSE VAHRFKDLGE ENFKALVLIA FAQYLQQCPF EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT VATLRETYGE MADCCAKQEP ERNECFLQHK DDNPNLPRLV RPEVDVMCTA FHDNEETFLK KYLYEIARRH PYFYAPELLF FAKRYKAAFT ECCQAADKAA CLLPKLDELR
*Corresponding author: Aibassov Yerkin Zhakenovich, professor, rearch field: organic chemistry of U, Th, As, Sb, Bi.E-mail:***************.DEGKASSAKQ RLKCASLQKF GERAFKAWAV ARLSQRFPKA EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF LGMFLYEYAR RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE FKPLVEEPQN LIKQNCELFE QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV LNQLCVLHEK TPVSDRVTKC CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL SEKERQIKKQ TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV AASQAALGL.
The italicized first 24 amino acids are signal and propeptide portions are not obrved in the translation, and transported protein but prent in the gene. There are 609 amino acids in this quence with only 585 amino acids in the final product obrved in the blood.
In work [1] has been studied chemical and biological insights into uranium-induced apoptosis of rat hepatic cell line. Uranium relea into the environment is a threat to human health, and the mechanisms of cytotoxicity caud by uranium are not well-understood. To improve our understanding in this
respect, the authors herein evaluate the effects of
All Rights Rerved.
Infrared Spectra and X-ray Examination of the Complex Albumin Human with UO 22+
325
uranium exposure on normal rat hepatic BRL cells. As revealed by SEM (scanning electron microscopy) and TEM (transmission electron microscope) analys, uranyl nitrate was found to be transformed into uranyl phosphate particles in the medium and taken up by BRL cells in an endocytotic uptake manner, which presumably initiates apoptosis of the cell, although soluble uranyl ion may also be toxic. The apoptosis of BRL cells upon uranium exposure was also confirmed by both the acridine orange and ethidium bromide double staining assay and the Annexin V/propidium iodide double staining assay. Further studies revealed that uranium induced the loss of mitochondrial membrane potential in a do-dependent manner. Moreover, the uranium-induced apoptosis was found to be associated with the activation of caspa-3, caspa-8 and caspa-9, indicating both a mitochondria-dependent signaling pathway and a death receptor pathway by a crosstalk. This study provides new chemical and biological insights into the mechanism of uranium toxicity toward hepatic cells,
which will help ek approaches for biological
remediation of uranium.
2. Experimental Sections
Dioxouranium (VI) (UO 22+) cation was ud as nitrate salts. Albumin human was ud as disodium salt. Reaction dioxouraniun (VI) UO 22+ ion with human rum albumin was prepared: human albumin with
uranium UO 22+ ion and the X-ray method of investigation of the complexes.
3. Results and Discussion
In work [1] has been studied structural conquences of Binding of UO 22+ to Apotransferrin. It has been established that transferrin binds a variety of metals. The include toxic uranyl ions which form rather stable uranyl-transferrin derivatives. The authors determined the extent to which the iron binding sites might accommodate the peculiar topographic profile of the uranyl ion and the conquences of its binding on protein conformation. Indeed, metal intake via endocytosis of the transferrin/transferring receptor depends on the adequate coordination of the metal in its site, which controls protein conformation and receptor binding. Using UV −vis and Fourier transform infrared difference spectroscopy coupled to a microdialysis system, the authors showed that at both metal binding sites two tyrosines are uranyl ligands, while histidine does not participate with its coordination sphere. Analysis by circular dichroism and DSC (differential scanning calorimetry) show
ed major differences between structural changes associated with interactions of iron or uranyl with apotransferrin. Uranyl coordination reduces the level of protein stabilization compared to iron, but this may be simply related to partial lobe closure. The lack of interaction between
Fig. 1 Structural conquences of binding of Fe 3+ and UO 22+
to Apotransferrin.
All Rights Rerved.
Infrared Spectra and X-ray Examination of the Complex Albumin Human with UO22+ 326
杨再兴uranyl-TF and its receptor was shown by flow cytometry using Alexa 488-labeled holotransferrin. The authors propo a structural model summarizing our conclusion that the uranyl-TF complex adopts an open conformation that is not appropriate for optimal binding to the transferrin receptor.
In work [2] has been studied UO22+ uptake by proteins. The capture of uranyl, UO22+, by a recently engineered protein with high lectivity and femtomolar nsitivity has been examined by a combination of density functional theory, molecular dynamics, and free-energy simulations. It was found that UO22+ is coordinated to five carboxylate oxygen atoms from four amino acid residues of t
he SUP (super uranyl binding protein). A network of hydrogen bonds between the amino acid residues coordinated to UO22+ and residues in its cond coordination sphere also affects the protein’s uranyl binding affinity. Free-energy simulations show how UO22+ capture is governed by the nature of the amino acid residues in the binding site, the integrity and strength of the cond-sphere hydrogen bond network, and the number of water molecules in the first coordination sphere. Alteration of any of the three factors through mutations generally results in a reduction of the binding free energy of UO22+ to the aqueous protein as well as of the difference between the binding free energies of UO22+ and other ions (Ca2+, Cu2+, Mg2+, and Zn2+), a proxy for the protein’s lectivity over the ions. The results of the free-energy simulations confirmed the previously reported experimental results and allowed us to discover a mutant of SUP, specifically the GLU64ASP mutant, that not only binds UO22+ more strongly than SUP but that is also more lective for UO22+ over other ions. The predictions from the computations were confirmed experimentally [3-5].
Analysis of the complex albumin human with uranium UO22+ ion was performed by X-ray microanalysis. Instrument: electron probe microanalyzer. Brand: Superprobe 733, Japan Electron Optics Laboratories, Japan.
The analysis of the elemental composition of the resulting of the microsphere magnetic catalyst with salts of Thorium and Uranium was performed using energy-dispersive spectrometer Energy Oxford Instruments, England, established by electron probe microanalyzer Superprobe 733 at an accelerating voltage of 25 kV and a probe current of 25 nA.
Figs. 2 and 3 show the laboratory unit and X-ray spectrum of the complex albumin human with UO22+. Table 1 shows the elemental composition of the complex albumin human with UO22+ ion.
Fig. 4 shows IR spectrum of the complex albumin human with UO22+.
Thus, the authors obtained a complex of albumin human with uranium UO22+ ions and IR spectra and
X-ray method to explore the complexes.
4. Conclusions
马斯卡彭奶酪Interaction of dioxouraniun (VI) UO22+ ion with albumin human was obtained a complex of adenosine with uranium UO22+ ion and X-ray method to explore the complexes.
虎斑心名词解释All Rights Rerved.
休学申请
Infrared Spectra and X-ray Examination of the Complex Albumin Human with UO 22+
327
梦见没赶上车
Fig. 2 Obtain a complex of albumin human with UO 22+
.
Fig. 3 X-ray spectrum of the complex albumin human with UO 22+
.
Table 1 Elemental composition of the complex albumin human with UO 22+.
Compound C H O N S P U Unit,
% 33.06 0.02
22.04 19.28 0.08 0.42 0.36
All Rights Rerved.
Infrared Spectra and X-ray Examination of the Complex Albumin Human with UO 22+
328
Fig. 4 IR spectrum of the complex albumin human with UO 22+
.
Acknowledgments
The authors would like to thank Lynn C.
Francesconi (Hunter College CUNY), Ruben M.
Savizky (Columbia University, New York), Peter C. Burns (Notre Dame University, Indiana) and Chistopher L. Cahill (George Washington University) for discussion of the results.
References
[1] Liu, F., Du, K. J., Fang, Z., You, Y., Wen, G. B., and Lin
Y. W. 2007. “Chemical and Biological Insights into Uranium-Induced Apoptosis of Rat Hepatic Cell Line.” Radiat Environ Biophys . 54 (2): 207-16. [2] Vidaud, C., Gourion-Arsiquaud, S., and Quemeneu, E.
2007. “Structural Conquences of Binding of UO 22+ to Apotransferrin: Can This Protein Account for Entry of Uranium into Human Cells?” Biochem. 46 (8): 2215-26. [3] Qi, L., Bast, C., and Vidand, C. 2014. “Characterization
of UO 22+ Binding to Osteopontin, a Highly Phosphorylated Protein: Insights into Potential Mechanisms of Uranyl Accumulation in Bones.” Metallomics 6: 166-76.
[4] Teniz, T. 2012. “Glutamic Acid Containing
Supermacroporous Poly(Hydroxyethyl Methacrylate) Cryogel Disks for UO 22+ Removal.” Materials Science and Eng . 32 (7): 2052-9.
[5] Yerkin, A., and Valentina, Y. 2015. Spin Chemistry and
Magnetic of Uranium-Thorium Catalysts . New York: Scientific & Academic Publishing, pp. 232.
4000 3500 3000 2500 2000 1500 1000
0.000 0.050
0.020
隧道英语
Wavenumber (cm -1)
0.015 0.010
A b s o r b a n c e (%) All Rights Rerved.
