High-throughput SANS experiment on two-detector system of YuMO spectrometer

Куклин, А. И.; Ivankov, A. I.; Soloviov, Dmytro; Rogachev, Andrey; Kovalev, Yu. S.; Soloviev, A. G.; Исламов, А. Х.; Bǎlǎșoiu, M.; Vlasov, A.V.; Kutuzov, S. A.; Sirotin, A. P.; Kirilov, A. S.; Skoi, V. V.; Rulev, Maksim; Gordeliy, Valentin

doi:10.1088/1742-6596/994/1/012016

Cited by 23 publications

(14 citation statements)

References 36 publications

(37 reference statements)

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“…Our SANS experiments performed at temperatures ensuing the variation of membrane thermodynamic properties suggest for the rst time dramatic changes to the structure of membrane organization due to Aβ 25-35 incorporation. The DPPC/Aβ 25-35 membranes undergo an initial transition from EULVs (outer diameter of 800 Å) to BLSs (outer diameter of 400 Å), and both DPPC/Aβ 25-35 and DMPC/Aβ [25][26][27][28][29][30][31][32][33][34][35] membranes transition reversibly between the BLSs and SULVs (outer diameter of 200Å) during their phase transitions. Our observations are consistent with membrane damage and its subsequent reformation being caused by the separate peptides or their small oligomers.…”

Section: Discussionmentioning

confidence: 99%

“…DMPC (1 wt%) and DMPC/Aβ [25][26][27][28][29][30][31][32][33][34][35] (1 wt% total, and 3 mol% of Aβ 25-35 ) solutions were diluted in deionized water to a nal concentration of 67 µg/ml. The samples were set on carbon-coated 200 mesh copper grids with a thin layer of carbon 10 nm.…”

Section: Methodsmentioning

confidence: 99%

“…Small angle neutron scattering experiments. SANS measurements were performed at the time-of-ight spectrometer YuMO at the IBR-2 pulsed reactor (JINR, Dubna, Russia) 31 . The beam of neutrons was formed by a set of two pinhole collimators of diameters 40 and 14 mm.…”

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Amyloid-beta peptide (25-35) triggers a reorganization of lipid membranes driven by temperature changes

Ivankov

Murugova

Ermakova

et al. 2021

Preprint

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The amyloid-beta peptide (Aβ) is considered a key factor in Alzheimer's disease (AD) ever since the discovery of the disease. The understanding of its damaging influence has however shifted recently from large fibrils observed in the inter-cellular environment to the small oligomers interacting with a cell membrane. We studied the effect of temperature on the latter interactions by evaluating the structural characteristics of zwitterionic phosphatidylcholine (PC) membranes with incorporated Aβ25-35 peptide. By means of small angle neutron scattering (SANS), we have observed for the first time a spontaneous reformation of extruded unilamellar vesicles (EULVs) to discoidal bicelle-like structures (BLSs) and small unilamellar vesicles (SULVs). These changes in the membrane self-organization happen during the thermodynamic phase transitions of lipids and only in the presence of the peptide. We interpret the dramatic changes in the membrane's overall shape with parallel changes in its thickness as the Aβ25-35 triggered membrane damage and a consequent reorganization of its structure. The suggested process is consistent with an action of separate peptides or a small number of peptide oligomers rather than the result of a large Aβ fibril.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Amyloid-beta peptide (25-35) triggers a reorganization of lipid membranes driven by temperature changes

Ivankov

Murugova

Ermakova

et al. 2021

Preprint

View full text Add to dashboard Cite

show abstract

“…Initial SAXS data processing was performed automatically using the EDNA pipeline (Brennich et al, 2016;Incardona et al, 2009). SANS experiments were performed using aYuMO SANS spectrometer in two-detector mode (Kuklin et al, 2005) located on beamline 4 of the IBR-2 pulsed reactor at the Joint Institute for Nuclear Research, Dubna, Russia (Kuklin et al, 2018). A vanadium standard was used for absolute cross-section normalization (Kuklin et al, 2017;Ostanevich, 1988).…”

Section: Saxs and Sans Measurementsmentioning

confidence: 99%

Ambiguities in and completeness of SAS data analysis of membrane proteins: the case of the sensory rhodopsin II–transducer complex

Ryzhykau¹,

Orekhov²,

Rulev³

et al. 2021

Acta Cryst Sect D Struct Biol

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Membrane proteins (MPs) play vital roles in the function of cells and are also major drug targets. Structural information on proteins is vital for understanding their mechanism of function and is critical for the development of drugs. However, obtaining high-resolution structures of membrane proteins, in particular, under native conditions is still a great challenge. In such cases, the low-resolution methods small-angle X-ray and neutron scattering (SAXS and SANS) might provide valuable structural information. However, in some cases small-angle scattering (SAS) provides ambiguous ab initio structural information if complementary measurements are not performed and/or a priori information on the protein is not taken into account. Understanding the nature of the limitations may help to overcome these problems. One of the main problems of SAS data analysis of solubilized membrane proteins is the contribution of the detergent belt surrounding the MP. Here, a comprehensive analysis of how the detergent belt contributes to the SAS data of a membrane-protein complex of sensory rhodopsin II with its cognate transducer from Natronomonas pharaonis (NpSRII–NpHtrII) was performed. The influence of the polydispersity of NpSRII–NpHtrII oligomerization is the second problem that is addressed here. It is shown that inhomogeneity in the scattering length density of the detergent belt surrounding a membrane part of the complex and oligomerization polydispersity significantly impacts on SAXS and SANS profiles, and therefore on 3D ab initio structures. It is described how both problems can be taken into account to improve the quality of SAS data treatment. Since SAS data for MPs are usually obtained from solubilized proteins, and their detergent belt and, to a certain extent, oligomerization polydispersity are sufficiently common phenomena, the approaches proposed in this work might be used in SAS studies of different MPs.

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“…SANS measurements were performed at the time-of-flight spectrometer YuMO at the IBR-2 pulsed reactor (JINR, Dubna, Russia) 34 . The beam of neutrons was formed by a set of two pinhole collimators of diameters 40 and 14 mm.…”

Section: Methodsmentioning

confidence: 99%

Amyloid-beta peptide (25–35) triggers a reorganization of lipid membranes driven by temperature changes

Ivankov

Murugova

Ermakova

et al. 2021

Sci Rep

View full text Add to dashboard Cite

The amyloid-beta peptide (Aβ) is considered a key factor in Alzheimer's disease (AD) ever since the discovery of the disease. The understanding of its damaging influence has however shifted recently from large fibrils observed in the inter-cellular environment to the small oligomers interacting with a cell membrane. We studied the effect of temperature on the latter interactions by evaluating the structural characteristics of zwitterionic phosphatidylcholine (PC) membranes with incorporated Aβ25–35 peptide. By means of small angle neutron scattering (SANS), we have observed for the first time a spontaneous reformation of extruded unilamellar vesicles (EULVs) to discoidal bicelle-like structures (BLSs) and small unilamellar vesicles (SULVs). These changes in the membrane self-organization happen during the thermodynamic phase transitions of lipids and only in the presence of the peptide. We interpret the dramatic changes in the membrane's overall shape with parallel changes in its thickness as the Aβ25–35 triggered membrane damage and a consequent reorganization of its structure. The suggested process is consistent with an action of separate peptides or small size peptide oligomers rather than the result of large Aβ fibrils.

show abstract

High-throughput SANS experiment on two-detector system of YuMO spectrometer

Cited by 23 publications

References 36 publications

Amyloid-beta peptide (25-35) triggers a reorganization of lipid membranes driven by temperature changes

Amyloid-beta peptide (25-35) triggers a reorganization of lipid membranes driven by temperature changes

Ambiguities in and completeness of SAS data analysis of membrane proteins: the case of the sensory rhodopsin II–transducer complex

Amyloid-beta peptide (25–35) triggers a reorganization of lipid membranes driven by temperature changes

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