Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $
Abstract Work with the Alzheimer’s disease-related synthetic peptide beta-amyloid (Aβ) is a challenging task because of its disadvantageous dissolution properties and high propensity for aggregation. Recently, a new synthetic derivative, iso-$ Aβ_{42} $, has been introduced, which is a precursor of...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Bogár, Ferenc [verfasserIn] Simon, Dóra [verfasserIn] Bozsó, Zsolt [verfasserIn] Janáky, Tamás [verfasserIn] Veszelka, Szilvia [verfasserIn] Tóth, Andrea E. [verfasserIn] Deli, Mária A. [verfasserIn] Borics, Attila [verfasserIn] Násztor, Zoltán [verfasserIn] Gyebrovszki, Andrea [verfasserIn] Penke, Botond [verfasserIn] Fülöp, Lívia [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Structural chemistry - Dordrecht : Springer Science Business Media B.V., 1990, 26(2015), 5-6 vom: 12. Sept., Seite 1389-1403 |
|---|---|
| Übergeordnetes Werk: |
volume:26 ; year:2015 ; number:5-6 ; day:12 ; month:09 ; pages:1389-1403 |
| Links: |
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| DOI / URN: |
10.1007/s11224-015-0660-2 |
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| Katalog-ID: |
SPR017886627 |
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| 245 | 1 | 0 | |a Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ |
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| 520 | |a Abstract Work with the Alzheimer’s disease-related synthetic peptide beta-amyloid (Aβ) is a challenging task because of its disadvantageous dissolution properties and high propensity for aggregation. Recently, a new synthetic derivative, iso-$ Aβ_{42} $, has been introduced, which is a precursor of $ Aβ_{42} $, and it offers advantages as concerns its synthesis and use for sample preparation. These two Aβ forms showed high similarity in their biological effects, as well as in their main structural characteristics under well-chosen experimental circumstances. When we changed these conditions, considerable dissimilarities appeared in the aggregation properties of the two peptides. In the present study, the aggregation pathways of native and precursor-derived $ Aβ_{42} $ oligomers were compared in a physiological buffer with and without divalent metal ions ($ Ca^{2+} $/$ Mg^{2+} $). The presence of these ions influenced the Aβ conformations, the morphology as well as formation dynamics of aggregates in a different manner, as it was demonstrated by thioflavin-T-binding experiments, transmission electron microscopy and electronic circular dichroism measurements. Namely, the aggregation of native $ Aβ_{42} $ to fibrils was facilitated, while the aggregation of precursor-derived $ Aβ_{42} $ was hindered by these divalent metal ions. The observed differences in the aggregation had an impact also on the biological efficiency of native and precursor-derived $ Aβ_{42} $ as it was elucidated by viability assays with enhanced sensitivity on primary endothelial cell cultures. Using replica exchange molecular dynamics, we modeled the conformational ensembles of the two investigated Aβ variants evolving during preparation process. We found considerable differences in the probability distribution of the conformers that can explain the observed dissimilarities in their aggregation properties. | ||
| 650 | 4 | |a Alzheimer’s disease |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Beta-amyloid aggregation |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Divalent metal ions |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Replica exchange molecular dynamics |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Simon, Dóra |e verfasserin |4 aut | |
| 700 | 1 | |a Bozsó, Zsolt |e verfasserin |4 aut | |
| 700 | 1 | |a Janáky, Tamás |e verfasserin |4 aut | |
| 700 | 1 | |a Veszelka, Szilvia |e verfasserin |4 aut | |
| 700 | 1 | |a Tóth, Andrea E. |e verfasserin |4 aut | |
| 700 | 1 | |a Deli, Mária A. |e verfasserin |4 aut | |
| 700 | 1 | |a Borics, Attila |e verfasserin |4 aut | |
| 700 | 1 | |a Násztor, Zoltán |e verfasserin |4 aut | |
| 700 | 1 | |a Gyebrovszki, Andrea |e verfasserin |4 aut | |
| 700 | 1 | |a Penke, Botond |e verfasserin |4 aut | |
| 700 | 1 | |a Fülöp, Lívia |e verfasserin |4 aut | |
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10.1007/s11224-015-0660-2 doi (DE-627)SPR017886627 (SPR)s11224-015-0660-2-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl Bogár, Ferenc verfasserin aut Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Work with the Alzheimer’s disease-related synthetic peptide beta-amyloid (Aβ) is a challenging task because of its disadvantageous dissolution properties and high propensity for aggregation. Recently, a new synthetic derivative, iso-$ Aβ_{42} $, has been introduced, which is a precursor of $ Aβ_{42} $, and it offers advantages as concerns its synthesis and use for sample preparation. These two Aβ forms showed high similarity in their biological effects, as well as in their main structural characteristics under well-chosen experimental circumstances. When we changed these conditions, considerable dissimilarities appeared in the aggregation properties of the two peptides. In the present study, the aggregation pathways of native and precursor-derived $ Aβ_{42} $ oligomers were compared in a physiological buffer with and without divalent metal ions ($ Ca^{2+} $/$ Mg^{2+} $). The presence of these ions influenced the Aβ conformations, the morphology as well as formation dynamics of aggregates in a different manner, as it was demonstrated by thioflavin-T-binding experiments, transmission electron microscopy and electronic circular dichroism measurements. Namely, the aggregation of native $ Aβ_{42} $ to fibrils was facilitated, while the aggregation of precursor-derived $ Aβ_{42} $ was hindered by these divalent metal ions. The observed differences in the aggregation had an impact also on the biological efficiency of native and precursor-derived $ Aβ_{42} $ as it was elucidated by viability assays with enhanced sensitivity on primary endothelial cell cultures. Using replica exchange molecular dynamics, we modeled the conformational ensembles of the two investigated Aβ variants evolving during preparation process. We found considerable differences in the probability distribution of the conformers that can explain the observed dissimilarities in their aggregation properties. Alzheimer’s disease (dpeaa)DE-He213 Beta-amyloid aggregation (dpeaa)DE-He213 Divalent metal ions (dpeaa)DE-He213 Replica exchange molecular dynamics (dpeaa)DE-He213 Simon, Dóra verfasserin aut Bozsó, Zsolt verfasserin aut Janáky, Tamás verfasserin aut Veszelka, Szilvia verfasserin aut Tóth, Andrea E. verfasserin aut Deli, Mária A. verfasserin aut Borics, Attila verfasserin aut Násztor, Zoltán verfasserin aut Gyebrovszki, Andrea verfasserin aut Penke, Botond verfasserin aut Fülöp, Lívia verfasserin aut Enthalten in Structural chemistry Dordrecht : Springer Science Business Media B.V., 1990 26(2015), 5-6 vom: 12. Sept., Seite 1389-1403 (DE-627)31886276X (DE-600)2018832-8 1572-9001 nnns volume:26 year:2015 number:5-6 day:12 month:09 pages:1389-1403 https://dx.doi.org/10.1007/s11224-015-0660-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE AR 26 2015 5-6 12 09 1389-1403 |
| spelling |
10.1007/s11224-015-0660-2 doi (DE-627)SPR017886627 (SPR)s11224-015-0660-2-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl Bogár, Ferenc verfasserin aut Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Work with the Alzheimer’s disease-related synthetic peptide beta-amyloid (Aβ) is a challenging task because of its disadvantageous dissolution properties and high propensity for aggregation. Recently, a new synthetic derivative, iso-$ Aβ_{42} $, has been introduced, which is a precursor of $ Aβ_{42} $, and it offers advantages as concerns its synthesis and use for sample preparation. These two Aβ forms showed high similarity in their biological effects, as well as in their main structural characteristics under well-chosen experimental circumstances. When we changed these conditions, considerable dissimilarities appeared in the aggregation properties of the two peptides. In the present study, the aggregation pathways of native and precursor-derived $ Aβ_{42} $ oligomers were compared in a physiological buffer with and without divalent metal ions ($ Ca^{2+} $/$ Mg^{2+} $). The presence of these ions influenced the Aβ conformations, the morphology as well as formation dynamics of aggregates in a different manner, as it was demonstrated by thioflavin-T-binding experiments, transmission electron microscopy and electronic circular dichroism measurements. Namely, the aggregation of native $ Aβ_{42} $ to fibrils was facilitated, while the aggregation of precursor-derived $ Aβ_{42} $ was hindered by these divalent metal ions. The observed differences in the aggregation had an impact also on the biological efficiency of native and precursor-derived $ Aβ_{42} $ as it was elucidated by viability assays with enhanced sensitivity on primary endothelial cell cultures. Using replica exchange molecular dynamics, we modeled the conformational ensembles of the two investigated Aβ variants evolving during preparation process. We found considerable differences in the probability distribution of the conformers that can explain the observed dissimilarities in their aggregation properties. Alzheimer’s disease (dpeaa)DE-He213 Beta-amyloid aggregation (dpeaa)DE-He213 Divalent metal ions (dpeaa)DE-He213 Replica exchange molecular dynamics (dpeaa)DE-He213 Simon, Dóra verfasserin aut Bozsó, Zsolt verfasserin aut Janáky, Tamás verfasserin aut Veszelka, Szilvia verfasserin aut Tóth, Andrea E. verfasserin aut Deli, Mária A. verfasserin aut Borics, Attila verfasserin aut Násztor, Zoltán verfasserin aut Gyebrovszki, Andrea verfasserin aut Penke, Botond verfasserin aut Fülöp, Lívia verfasserin aut Enthalten in Structural chemistry Dordrecht : Springer Science Business Media B.V., 1990 26(2015), 5-6 vom: 12. Sept., Seite 1389-1403 (DE-627)31886276X (DE-600)2018832-8 1572-9001 nnns volume:26 year:2015 number:5-6 day:12 month:09 pages:1389-1403 https://dx.doi.org/10.1007/s11224-015-0660-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE AR 26 2015 5-6 12 09 1389-1403 |
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10.1007/s11224-015-0660-2 doi (DE-627)SPR017886627 (SPR)s11224-015-0660-2-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl Bogár, Ferenc verfasserin aut Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Work with the Alzheimer’s disease-related synthetic peptide beta-amyloid (Aβ) is a challenging task because of its disadvantageous dissolution properties and high propensity for aggregation. Recently, a new synthetic derivative, iso-$ Aβ_{42} $, has been introduced, which is a precursor of $ Aβ_{42} $, and it offers advantages as concerns its synthesis and use for sample preparation. These two Aβ forms showed high similarity in their biological effects, as well as in their main structural characteristics under well-chosen experimental circumstances. When we changed these conditions, considerable dissimilarities appeared in the aggregation properties of the two peptides. In the present study, the aggregation pathways of native and precursor-derived $ Aβ_{42} $ oligomers were compared in a physiological buffer with and without divalent metal ions ($ Ca^{2+} $/$ Mg^{2+} $). The presence of these ions influenced the Aβ conformations, the morphology as well as formation dynamics of aggregates in a different manner, as it was demonstrated by thioflavin-T-binding experiments, transmission electron microscopy and electronic circular dichroism measurements. Namely, the aggregation of native $ Aβ_{42} $ to fibrils was facilitated, while the aggregation of precursor-derived $ Aβ_{42} $ was hindered by these divalent metal ions. The observed differences in the aggregation had an impact also on the biological efficiency of native and precursor-derived $ Aβ_{42} $ as it was elucidated by viability assays with enhanced sensitivity on primary endothelial cell cultures. Using replica exchange molecular dynamics, we modeled the conformational ensembles of the two investigated Aβ variants evolving during preparation process. We found considerable differences in the probability distribution of the conformers that can explain the observed dissimilarities in their aggregation properties. Alzheimer’s disease (dpeaa)DE-He213 Beta-amyloid aggregation (dpeaa)DE-He213 Divalent metal ions (dpeaa)DE-He213 Replica exchange molecular dynamics (dpeaa)DE-He213 Simon, Dóra verfasserin aut Bozsó, Zsolt verfasserin aut Janáky, Tamás verfasserin aut Veszelka, Szilvia verfasserin aut Tóth, Andrea E. verfasserin aut Deli, Mária A. verfasserin aut Borics, Attila verfasserin aut Násztor, Zoltán verfasserin aut Gyebrovszki, Andrea verfasserin aut Penke, Botond verfasserin aut Fülöp, Lívia verfasserin aut Enthalten in Structural chemistry Dordrecht : Springer Science Business Media B.V., 1990 26(2015), 5-6 vom: 12. Sept., Seite 1389-1403 (DE-627)31886276X (DE-600)2018832-8 1572-9001 nnns volume:26 year:2015 number:5-6 day:12 month:09 pages:1389-1403 https://dx.doi.org/10.1007/s11224-015-0660-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE AR 26 2015 5-6 12 09 1389-1403 |
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10.1007/s11224-015-0660-2 doi (DE-627)SPR017886627 (SPR)s11224-015-0660-2-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl Bogár, Ferenc verfasserin aut Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Work with the Alzheimer’s disease-related synthetic peptide beta-amyloid (Aβ) is a challenging task because of its disadvantageous dissolution properties and high propensity for aggregation. Recently, a new synthetic derivative, iso-$ Aβ_{42} $, has been introduced, which is a precursor of $ Aβ_{42} $, and it offers advantages as concerns its synthesis and use for sample preparation. These two Aβ forms showed high similarity in their biological effects, as well as in their main structural characteristics under well-chosen experimental circumstances. When we changed these conditions, considerable dissimilarities appeared in the aggregation properties of the two peptides. In the present study, the aggregation pathways of native and precursor-derived $ Aβ_{42} $ oligomers were compared in a physiological buffer with and without divalent metal ions ($ Ca^{2+} $/$ Mg^{2+} $). The presence of these ions influenced the Aβ conformations, the morphology as well as formation dynamics of aggregates in a different manner, as it was demonstrated by thioflavin-T-binding experiments, transmission electron microscopy and electronic circular dichroism measurements. Namely, the aggregation of native $ Aβ_{42} $ to fibrils was facilitated, while the aggregation of precursor-derived $ Aβ_{42} $ was hindered by these divalent metal ions. The observed differences in the aggregation had an impact also on the biological efficiency of native and precursor-derived $ Aβ_{42} $ as it was elucidated by viability assays with enhanced sensitivity on primary endothelial cell cultures. Using replica exchange molecular dynamics, we modeled the conformational ensembles of the two investigated Aβ variants evolving during preparation process. We found considerable differences in the probability distribution of the conformers that can explain the observed dissimilarities in their aggregation properties. Alzheimer’s disease (dpeaa)DE-He213 Beta-amyloid aggregation (dpeaa)DE-He213 Divalent metal ions (dpeaa)DE-He213 Replica exchange molecular dynamics (dpeaa)DE-He213 Simon, Dóra verfasserin aut Bozsó, Zsolt verfasserin aut Janáky, Tamás verfasserin aut Veszelka, Szilvia verfasserin aut Tóth, Andrea E. verfasserin aut Deli, Mária A. verfasserin aut Borics, Attila verfasserin aut Násztor, Zoltán verfasserin aut Gyebrovszki, Andrea verfasserin aut Penke, Botond verfasserin aut Fülöp, Lívia verfasserin aut Enthalten in Structural chemistry Dordrecht : Springer Science Business Media B.V., 1990 26(2015), 5-6 vom: 12. Sept., Seite 1389-1403 (DE-627)31886276X (DE-600)2018832-8 1572-9001 nnns volume:26 year:2015 number:5-6 day:12 month:09 pages:1389-1403 https://dx.doi.org/10.1007/s11224-015-0660-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE AR 26 2015 5-6 12 09 1389-1403 |
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10.1007/s11224-015-0660-2 doi (DE-627)SPR017886627 (SPR)s11224-015-0660-2-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl Bogár, Ferenc verfasserin aut Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Work with the Alzheimer’s disease-related synthetic peptide beta-amyloid (Aβ) is a challenging task because of its disadvantageous dissolution properties and high propensity for aggregation. Recently, a new synthetic derivative, iso-$ Aβ_{42} $, has been introduced, which is a precursor of $ Aβ_{42} $, and it offers advantages as concerns its synthesis and use for sample preparation. These two Aβ forms showed high similarity in their biological effects, as well as in their main structural characteristics under well-chosen experimental circumstances. When we changed these conditions, considerable dissimilarities appeared in the aggregation properties of the two peptides. In the present study, the aggregation pathways of native and precursor-derived $ Aβ_{42} $ oligomers were compared in a physiological buffer with and without divalent metal ions ($ Ca^{2+} $/$ Mg^{2+} $). The presence of these ions influenced the Aβ conformations, the morphology as well as formation dynamics of aggregates in a different manner, as it was demonstrated by thioflavin-T-binding experiments, transmission electron microscopy and electronic circular dichroism measurements. Namely, the aggregation of native $ Aβ_{42} $ to fibrils was facilitated, while the aggregation of precursor-derived $ Aβ_{42} $ was hindered by these divalent metal ions. The observed differences in the aggregation had an impact also on the biological efficiency of native and precursor-derived $ Aβ_{42} $ as it was elucidated by viability assays with enhanced sensitivity on primary endothelial cell cultures. Using replica exchange molecular dynamics, we modeled the conformational ensembles of the two investigated Aβ variants evolving during preparation process. We found considerable differences in the probability distribution of the conformers that can explain the observed dissimilarities in their aggregation properties. Alzheimer’s disease (dpeaa)DE-He213 Beta-amyloid aggregation (dpeaa)DE-He213 Divalent metal ions (dpeaa)DE-He213 Replica exchange molecular dynamics (dpeaa)DE-He213 Simon, Dóra verfasserin aut Bozsó, Zsolt verfasserin aut Janáky, Tamás verfasserin aut Veszelka, Szilvia verfasserin aut Tóth, Andrea E. verfasserin aut Deli, Mária A. verfasserin aut Borics, Attila verfasserin aut Násztor, Zoltán verfasserin aut Gyebrovszki, Andrea verfasserin aut Penke, Botond verfasserin aut Fülöp, Lívia verfasserin aut Enthalten in Structural chemistry Dordrecht : Springer Science Business Media B.V., 1990 26(2015), 5-6 vom: 12. Sept., Seite 1389-1403 (DE-627)31886276X (DE-600)2018832-8 1572-9001 nnns volume:26 year:2015 number:5-6 day:12 month:09 pages:1389-1403 https://dx.doi.org/10.1007/s11224-015-0660-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE AR 26 2015 5-6 12 09 1389-1403 |
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Enthalten in Structural chemistry 26(2015), 5-6 vom: 12. Sept., Seite 1389-1403 volume:26 year:2015 number:5-6 day:12 month:09 pages:1389-1403 |
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Alzheimer’s disease Beta-amyloid aggregation Divalent metal ions Replica exchange molecular dynamics |
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Bogár, Ferenc @@aut@@ Simon, Dóra @@aut@@ Bozsó, Zsolt @@aut@@ Janáky, Tamás @@aut@@ Veszelka, Szilvia @@aut@@ Tóth, Andrea E. @@aut@@ Deli, Mária A. @@aut@@ Borics, Attila @@aut@@ Násztor, Zoltán @@aut@@ Gyebrovszki, Andrea @@aut@@ Penke, Botond @@aut@@ Fülöp, Lívia @@aut@@ |
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Recently, a new synthetic derivative, iso-$ Aβ_{42} $, has been introduced, which is a precursor of $ Aβ_{42} $, and it offers advantages as concerns its synthesis and use for sample preparation. These two Aβ forms showed high similarity in their biological effects, as well as in their main structural characteristics under well-chosen experimental circumstances. When we changed these conditions, considerable dissimilarities appeared in the aggregation properties of the two peptides. In the present study, the aggregation pathways of native and precursor-derived $ Aβ_{42} $ oligomers were compared in a physiological buffer with and without divalent metal ions ($ Ca^{2+} $/$ Mg^{2+} $). The presence of these ions influenced the Aβ conformations, the morphology as well as formation dynamics of aggregates in a different manner, as it was demonstrated by thioflavin-T-binding experiments, transmission electron microscopy and electronic circular dichroism measurements. Namely, the aggregation of native $ Aβ_{42} $ to fibrils was facilitated, while the aggregation of precursor-derived $ Aβ_{42} $ was hindered by these divalent metal ions. The observed differences in the aggregation had an impact also on the biological efficiency of native and precursor-derived $ Aβ_{42} $ as it was elucidated by viability assays with enhanced sensitivity on primary endothelial cell cultures. Using replica exchange molecular dynamics, we modeled the conformational ensembles of the two investigated Aβ variants evolving during preparation process. 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| author |
Bogár, Ferenc |
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Bogár, Ferenc ddc 540 bkl 35.00 misc Alzheimer’s disease misc Beta-amyloid aggregation misc Divalent metal ions misc Replica exchange molecular dynamics Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ |
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540 ASE 35.00 bkl Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ Alzheimer’s disease (dpeaa)DE-He213 Beta-amyloid aggregation (dpeaa)DE-He213 Divalent metal ions (dpeaa)DE-He213 Replica exchange molecular dynamics (dpeaa)DE-He213 |
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ddc 540 bkl 35.00 misc Alzheimer’s disease misc Beta-amyloid aggregation misc Divalent metal ions misc Replica exchange molecular dynamics |
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ddc 540 bkl 35.00 misc Alzheimer’s disease misc Beta-amyloid aggregation misc Divalent metal ions misc Replica exchange molecular dynamics |
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ddc 540 bkl 35.00 misc Alzheimer’s disease misc Beta-amyloid aggregation misc Divalent metal ions misc Replica exchange molecular dynamics |
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Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ |
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Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ |
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Bogár, Ferenc |
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Structural chemistry |
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Bogár, Ferenc Simon, Dóra Bozsó, Zsolt Janáky, Tamás Veszelka, Szilvia Tóth, Andrea E. Deli, Mária A. Borics, Attila Násztor, Zoltán Gyebrovszki, Andrea Penke, Botond Fülöp, Lívia |
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Bogár, Ferenc |
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10.1007/s11224-015-0660-2 |
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| title_sort |
opposite effect of $ ca^{2+} $/$ mg^{2+} $ ions on the aggregation of native and precursor-derived $ aβ_{42} $ |
| title_auth |
Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ |
| abstract |
Abstract Work with the Alzheimer’s disease-related synthetic peptide beta-amyloid (Aβ) is a challenging task because of its disadvantageous dissolution properties and high propensity for aggregation. Recently, a new synthetic derivative, iso-$ Aβ_{42} $, has been introduced, which is a precursor of $ Aβ_{42} $, and it offers advantages as concerns its synthesis and use for sample preparation. These two Aβ forms showed high similarity in their biological effects, as well as in their main structural characteristics under well-chosen experimental circumstances. When we changed these conditions, considerable dissimilarities appeared in the aggregation properties of the two peptides. In the present study, the aggregation pathways of native and precursor-derived $ Aβ_{42} $ oligomers were compared in a physiological buffer with and without divalent metal ions ($ Ca^{2+} $/$ Mg^{2+} $). The presence of these ions influenced the Aβ conformations, the morphology as well as formation dynamics of aggregates in a different manner, as it was demonstrated by thioflavin-T-binding experiments, transmission electron microscopy and electronic circular dichroism measurements. Namely, the aggregation of native $ Aβ_{42} $ to fibrils was facilitated, while the aggregation of precursor-derived $ Aβ_{42} $ was hindered by these divalent metal ions. The observed differences in the aggregation had an impact also on the biological efficiency of native and precursor-derived $ Aβ_{42} $ as it was elucidated by viability assays with enhanced sensitivity on primary endothelial cell cultures. Using replica exchange molecular dynamics, we modeled the conformational ensembles of the two investigated Aβ variants evolving during preparation process. We found considerable differences in the probability distribution of the conformers that can explain the observed dissimilarities in their aggregation properties. |
| abstractGer |
Abstract Work with the Alzheimer’s disease-related synthetic peptide beta-amyloid (Aβ) is a challenging task because of its disadvantageous dissolution properties and high propensity for aggregation. Recently, a new synthetic derivative, iso-$ Aβ_{42} $, has been introduced, which is a precursor of $ Aβ_{42} $, and it offers advantages as concerns its synthesis and use for sample preparation. These two Aβ forms showed high similarity in their biological effects, as well as in their main structural characteristics under well-chosen experimental circumstances. When we changed these conditions, considerable dissimilarities appeared in the aggregation properties of the two peptides. In the present study, the aggregation pathways of native and precursor-derived $ Aβ_{42} $ oligomers were compared in a physiological buffer with and without divalent metal ions ($ Ca^{2+} $/$ Mg^{2+} $). The presence of these ions influenced the Aβ conformations, the morphology as well as formation dynamics of aggregates in a different manner, as it was demonstrated by thioflavin-T-binding experiments, transmission electron microscopy and electronic circular dichroism measurements. Namely, the aggregation of native $ Aβ_{42} $ to fibrils was facilitated, while the aggregation of precursor-derived $ Aβ_{42} $ was hindered by these divalent metal ions. The observed differences in the aggregation had an impact also on the biological efficiency of native and precursor-derived $ Aβ_{42} $ as it was elucidated by viability assays with enhanced sensitivity on primary endothelial cell cultures. Using replica exchange molecular dynamics, we modeled the conformational ensembles of the two investigated Aβ variants evolving during preparation process. We found considerable differences in the probability distribution of the conformers that can explain the observed dissimilarities in their aggregation properties. |
| abstract_unstemmed |
Abstract Work with the Alzheimer’s disease-related synthetic peptide beta-amyloid (Aβ) is a challenging task because of its disadvantageous dissolution properties and high propensity for aggregation. Recently, a new synthetic derivative, iso-$ Aβ_{42} $, has been introduced, which is a precursor of $ Aβ_{42} $, and it offers advantages as concerns its synthesis and use for sample preparation. These two Aβ forms showed high similarity in their biological effects, as well as in their main structural characteristics under well-chosen experimental circumstances. When we changed these conditions, considerable dissimilarities appeared in the aggregation properties of the two peptides. In the present study, the aggregation pathways of native and precursor-derived $ Aβ_{42} $ oligomers were compared in a physiological buffer with and without divalent metal ions ($ Ca^{2+} $/$ Mg^{2+} $). The presence of these ions influenced the Aβ conformations, the morphology as well as formation dynamics of aggregates in a different manner, as it was demonstrated by thioflavin-T-binding experiments, transmission electron microscopy and electronic circular dichroism measurements. Namely, the aggregation of native $ Aβ_{42} $ to fibrils was facilitated, while the aggregation of precursor-derived $ Aβ_{42} $ was hindered by these divalent metal ions. The observed differences in the aggregation had an impact also on the biological efficiency of native and precursor-derived $ Aβ_{42} $ as it was elucidated by viability assays with enhanced sensitivity on primary endothelial cell cultures. Using replica exchange molecular dynamics, we modeled the conformational ensembles of the two investigated Aβ variants evolving during preparation process. We found considerable differences in the probability distribution of the conformers that can explain the observed dissimilarities in their aggregation properties. |
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| title_short |
Opposite effect of $ Ca^{2+} $/$ Mg^{2+} $ ions on the aggregation of native and precursor-derived $ Aβ_{42} $ |
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https://dx.doi.org/10.1007/s11224-015-0660-2 |
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Simon, Dóra Bozsó, Zsolt Janáky, Tamás Veszelka, Szilvia Tóth, Andrea E. Deli, Mária A. Borics, Attila Násztor, Zoltán Gyebrovszki, Andrea Penke, Botond Fülöp, Lívia |
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| score |
7.3985376 |