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- Baranovskiy, A. E., et al.
(författare)
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Electronic structure, bulk and magnetic properties of MB6 and MB12 borides
- 2007
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Ingår i: Journal of Alloys and Compounds. - : Elsevier BV. - 0925-8388 .- 1873-4669. ; 442:1-2, s. 228-230
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Tidskriftsartikel (refereegranskat)abstract
- The bulk and magnetic properties of MB6 and MB12 were investigated on the basis of first principles electronic structure calculations. The elastic constants were measured for ZrB12, HoB12, ErB12, TmB12, LuB12, YB6 and LaB6 compounds at low temperatures. The calculated equations of states and balanced crystal orbital overlap populations have allowed to analyse bonding and magnetic properties of MB6 and MB12 .
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| 5. |
- Filippov, A. V., et al.
(författare)
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Effect of freezing on amyloid peptide aggregation and self-diffusion in an aqueous solution
- 2008
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Ingår i: Colloid Journal of the Russian Academy of Science. - 1061-933X .- 1608-3067. ; 70:4, s. 501-506
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Tidskriftsartikel (refereegranskat)abstract
- Pulsed-field gradient 1H NMR is employed to investigate the self-diffusion of amyloid Aβ-peptide in an aqueous buffer solution (pH 7.44) with a protein concentration of 50 μmol at 20°C. The self-diffusion coefficient of the peptide in a freshly prepared solution corresponds to its monomeric form. The storage of the solution at 24°C causes part of the peptide molecules to form amyloid aggregates as soon as over 48 h. However, the 1H NMR echo signal typical of aggregated molecules is not observed because of their dense packing in the aggregates and a large mass of the latter. A freezing-fusion of the solution after the aggregation does not cause changes in the self-diffusion coefficients of the peptide. After a peptide solution free of amyloid aggregates is subjected to a freezing-fusion cycle, part of the peptide molecules also remains in the monomeric form in the solution, while another part forms amyloid aggregates, with a portion of the aggregated peptide molecules retaining a high rotational mobility with virtually absolute absence of a translational mobility. The results obtained are interpreted in terms of the formation of "porous aggregates" of amyloid fibrils, with "pores" having sizes comparable with those of peptide molecules, though, being larger than water molecules. Peptide molecules, which do not form fibrils, are captured in the pores. Temperature regime is shown to be of importance for the aggregation of amyloid peptides. In particular, freezing, which is traditionally considered to be a method for the prevention from or temporary interruption of aggregation, may itself lead to the formation of amorphous amyloid aggregates, which remain preserved in solutions after their unfreezing.
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| 6. |
- Filippov, A V, et al.
(författare)
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Lateral Diffusion of Saturated Phosphatidylcholines in Cholesterol-containing Bilayers
- 2007
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Ingår i: Biophysics. - 0006-3509. ; 52:3, s. 307-14
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Tidskriftsartikel (refereegranskat)abstract
- A pulsed field gradient NMR was used to study lateral diffusion in the cholesterol-containing oriented bilayers of saturated (dipalmitoyl- and dimyristoyl-) phosphatidylcholines, upon their limiting hydration. Similar dependences of lateral diffusion coefficients on temperature and cholesterol concentration were observed, which agree with phase diagram showing the presence of the regions of disordered and ordered liquid-crystalline phases and a two-phase region. Under the same conditions, the lateral diffusion coefficient of dipalmitoylphosphatidylcholine is lower, which agrees qualitatively with its larger molecular weight. The comparison of data for dipalmitoylphosphatidylcholine with previous results for dipalmitoylsphingomyelin−cholesterol bilayers under the same conditions, in spite of similarity of phase diagrams, shows large (two−three times) differences in the lateral diffusion coefficient and a different profile of its dependence on cholesterol concentration. The comparison of data for dimyristoylphosphatidylcholine with previous results shows that the values of lateral diffusion coefficient and the shape of its dependence on cholesterol concentration coincide at high concentrations (>15 mol%) but differ at lower concentrations The revealed disagreement may be caused by the fact that the measurements were carried out at different water content in the system. At limiting hydration (more than 35% of water), the lateral diffusion coefficient for lipids decreases when cholesterol concentration rises, while at water content about 25% (as a result of equilibrium hydration from vapors) the lateral diffusion coefficient of phosphatidylcholine may be independent of cholesterol concentration. This is the consequence of the denser packing of molecules in the bilayer at reduced water content, an effect that competes with the ordering effect of cholesterol.
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| 7. |
- Grechnev, G. E., et al.
(författare)
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Electronic structure and bulk properties of MB6 and MB12 borides
- 2008
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Ingår i: Low temperature physics (Woodbury, N.Y., Print). - : AIP Publishing. - 1063-777X .- 1090-6517. ; 34:11, s. 921-929
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Tidskriftsartikel (refereegranskat)abstract
- Ab initio band structure calculations are carried out for the higher borides MB6 and MB12. High-precision measurements of the elastic constants are performed for the compounds ZrB12, HoB12, ErB12, TmB12, LuB12, YB6 and LaB6 at low temperatures. The bulk properties of the borides are analyzed on the basis of the calculated equations of states and balanced crystal orbital overlap populations. Our calculations indicate that hexaborides with divalent metals, CaB6, SrB6, BaB6, and YbB6, are semiconductors with small energy gaps. The metallic MB6 hexaborides with trivalent M atoms are found to possess larger bulk moduli values. For dodecaborides the bulk moduli are found to be higher for MB12 with increased filling of the conduction band (ZrB12, HfB12, UB12) in comparison with M3+B12 compounds. The total energy calculations for different magnetic configurations in YbB12 point to the possibility of antiferromagnetic coupling between Yb3+ ions.
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- Antzutkin, Oleg, et al.
(författare)
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Exploring solid-state 17O NMR to distinguish secondary structures in Alzheimer's Aβ fibrils
- 2009
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Ingår i: Euromar 2009. ; , s. 107-
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Konferensbidrag (övrigt vetenskapligt/konstnärligt)abstract
- It has been shown by a large number of studies that Alzheimer's disease (AD) amyloid-β-peptide (Aβ) deposits contribute directly to the disease's progressive neurodegeneration. Aggregation cascade for Aβ peptides, its relevance to neurotoxicity in the course of AD, various factors modulating Aβ aggregation kinetics and experimental methods useful for these studies were recently discussed [1]. Results of Tycko and co-workers point at neurotoxicity in vitro of the two different types of Alzheimer's amyloid fibrils dispersed by ultrasonication into small fragments [2]. The high toxicity of Aβ oligomers in vitro has been discussed by Stege et. al who have found that the molecular chaperone αB-crystallin prevents Aβ from forming amyloid fibrils but nevertheless enhances Aβ toxicity [3]. Glabe and co-workes successfully prepared antibodies for Aβ oligomers and small spherical aggregates using nanogold technology [4]. They also have shown that these antibodies decrease toxicity of Aβ for SH-SY5Y human neuroblastoma cell cultures in vitro [4]. In this concern both structure of Aβ-oligomers/fibrils and the specific interaction (aggregation/fusion) of Aβ peptides with nerve cell membranes is of a particular importance [5].We explore Solid-State 17O NMR on selectively 17O,13C,15N-labeled Aβ(1-40), Aβ(11-25) and Ac-Aβ(16-22)-NH2 peptides to distinguish a parallel and anti-parallel β-sheet secondary structures in β-NH2 peptides to distinguish a parallel and anti-parallel β-sheet secondary structures in amyloid fibrils. Aβ(1-40) fibrils form in-registry parallel β-sheets [6], while Aβ(11-25) [7] and Ac-Aβ(16-22)-NH2 [8] form different anti-parallel β-sheet structures, which were previously identified β-NH2 [8] form different anti-parallel β-sheet structures, which were previously identified by 13C multiple-quantum and 13C{15N} REDOR solid-state NMR. In our unpublished work presented here it was found that 17O NMR chemical shifts are sensitive to the type of the secondary structure, i. e. a parallel vs. an anti-parallel β-sheet structures, while the quadrupolar parameters of 17O nuclei unexpectedly do not vary beyond the error limits in the simulated lineshapes of both fibrillized and unfibrillized peptide systems. Results of more advanced solidstate NMR techniques to measure heteronuclear distances, 15N{17O}-REAPDOR, 15N{17O}-TRAPDOR and 17O{15N}-REDOR on selectively 17O-Val18 and 15N-Phe20 labeled Ac-Aβ(16-22)-NH2 fibrils will be also discussed. These novel solid-state NMR experiments will provide additional tools for measuring hydrogen bonding in different secondary structures of peptides in amyloid fibrils.[1.] O.N.Antzutkin, Magn. Reson. Chem. 42 (2004) 231-246; [2.] A.Petkova et al. Science 307 (2005) 262-265; [3.] G.J.J.Stege, et al. Biochem. Biophys. Res. Comm., 262 (1999) 152-156;[4.] R.Kayed et al. Science, 300 (2003) 486-489; [5.] M.Bokvist, et al. J. Mol. Biol. 335 (2004) 1039-1049; [6.] O.N. Antzutkin, et al. Proc. Nat. Acad. Sci, U.S.A., 97 (2000) 13045-13050;[7.] A.T. Petkova, et al. J. Mol. Biol., 335 (2004) 247-260;[8.] J.J. Balbach, Y. (2000) 13045-13050; [9] A.T. Petkova, (2004) 247-260; [10] J.J. Balbach, Y.Ishii, O.N. Antzutkin, et al. Biochemistry 39 (2000) 13748-13759.
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| 10. |
- Filippov, Andrei, et al.
(författare)
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Aggregation on an amyloid peptide as studied by NMR diffusometry and 2D NMR noesy spectroscopy
- 2009
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Ingår i: Protein folds in infectious and neurodegenerative diseases. - : Centre National de la Recherche Scientifique, CNRS. ; , s. 91-
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Konferensbidrag (övrigt vetenskapligt/konstnärligt)abstract
- Alzheimer's disease is a progressive neurodegenerative disorder affecting millions of people world-wide. Alzheimer's amyloid-b peptide forms amorphous aggregates or amyloid fibrils. However, recent studies indicate that soluble oligomers instead of fibrils may form probably most neurotoxic species. These oligomeric aggregates are difficult to study by traditional structural experimental techniques. NMR diffusometry offer useful additional possibilities. In freshly-prepared solutions (without any pre-aggregates of the peptide) diffusion of the peptide can often be described by an unique diffusion kinetics, which corresponds to the calculated diffusion coefficient of the amyloid- b peptide monomers with the Stokes-Einstein hard-sphere approximation (typically D ~10-10 m2/s). In a quasi-equilibrium or in pulse-induced conditions, new larger aggregates of Ab with diffusion coefficients down to <1×10-13 m2/s were detected. 2D 1H NMR NOESY provides both an additional evidence of aggregation and also reveals most probable sites of the side chain interactions in the aggregates. "Pulse-like" treatment of the sample involves: (i) changing of the solution composition; (ii) freezing-thawing; and (iii) sonication of the sample in the course of its incubation. Putative aggregation mechanisms and structures of monomers and oligomers in solutions at different conditions are discussed.1. Filippov A., Sulejmanova A., Antzutkin O. and Gröbner G. (2005) Diffusion and aggregation of Alzheimer's Abeta(1-40)-peptide in aqueous-TFE solutions as studied by pulsed field gradient NMR. Applied Magnetic Resonance. 29. 439 - 449.2. Filippov A., Sulejmanova A., Gröbner G. and Antzutkin O. (2008) Effect of freezing on amyloid peptide aggregation and self-diffusion in an aqueous solution. Colloid J. 70. 501-506.3. Filippov A., Gröbner G. and Antzutkin O. Effect of ultrasonication on amyloid peptide aggregation in trifluoroethanol solution. (in preparation).
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