Bis(sulfosuccinimidyl) suberate (BS3) crosslinking analysis of the behavior of amyloid-β peptide in solution and in phospholipid membranes
The structure and state of amyloid-β peptide (Aβ) oligomers often need to be checked by reliable experimental methods. Electrophoresis is a commonly applied measurement method. However, due to the presence of detergents, oligomers are easily broken during electrophoresis, which makes it very hard to...
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| Veröffentlicht in: | PloS one 2017-03, Vol.12 (3), p.e0173871-e0173871 |
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| creator | Shi, Jing-Ming Pei, Jie Liu, En-Qi Zhang, Lin |
| description | The structure and state of amyloid-β peptide (Aβ) oligomers often need to be checked by reliable experimental methods. Electrophoresis is a commonly applied measurement method. However, due to the presence of detergents, oligomers are easily broken during electrophoresis, which makes it very hard to accurately assess Aβ aggregate states. In the current study, bis(sulfosuccinimidyl) suberate (BS3) was used to cross-link Aβ1-42 oligomers prior to electrophoresis. When compared to a previously reported Aβ cross-linking agent, glutaraldehyde, it was quite apparent that BS3 is more suitable for detecting intra-membrane Aβ oligomers and extra-membrane Aβ oligomers states. As such, our findings provide an efficient method for analyzing Aβ proteins or other proteins that are easily aggregated in solution and in phospholipid membranes. |
| doi_str_mv | 10.1371/journal.pone.0173871 |
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Electrophoresis is a commonly applied measurement method. However, due to the presence of detergents, oligomers are easily broken during electrophoresis, which makes it very hard to accurately assess Aβ aggregate states. In the current study, bis(sulfosuccinimidyl) suberate (BS3) was used to cross-link Aβ1-42 oligomers prior to electrophoresis. When compared to a previously reported Aβ cross-linking agent, glutaraldehyde, it was quite apparent that BS3 is more suitable for detecting intra-membrane Aβ oligomers and extra-membrane Aβ oligomers states. As such, our findings provide an efficient method for analyzing Aβ proteins or other proteins that are easily aggregated in solution and in phospholipid membranes.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0173871</identifier><identifier>PMID: 28323849</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Alzheimer Disease - etiology ; Alzheimer Disease - metabolism ; Alzheimer's disease ; Alzheimers disease ; Amyloid beta-Peptides - chemistry ; Amyloid beta-Peptides - ultrastructure ; Biology and Life Sciences ; Cross-Linking Reagents ; Crosslinking ; Dementia ; Detergents ; Electrophoresis ; Epidermal growth factor ; Experimental methods ; Glutaral ; Glutaraldehyde ; Humans ; Ligands ; Medicine and Health Sciences ; Membranes ; Membranes, Artificial ; Microscopy ; Microscopy, Electron, Transmission ; Oligomers ; Pathogenesis ; Peptide Fragments - chemistry ; Peptide Fragments - ultrastructure ; Peptides ; Phospholipids ; Physical Sciences ; Protein Aggregates ; Protein Aggregation, Pathological - etiology ; Protein Aggregation, Pathological - metabolism ; Proteins ; Research and Analysis Methods ; Solutions ; Succinimides ; Toxicity ; β-Amyloid</subject><ispartof>PloS one, 2017-03, Vol.12 (3), p.e0173871-e0173871</ispartof><rights>2017 Shi et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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Electrophoresis is a commonly applied measurement method. However, due to the presence of detergents, oligomers are easily broken during electrophoresis, which makes it very hard to accurately assess Aβ aggregate states. In the current study, bis(sulfosuccinimidyl) suberate (BS3) was used to cross-link Aβ1-42 oligomers prior to electrophoresis. When compared to a previously reported Aβ cross-linking agent, glutaraldehyde, it was quite apparent that BS3 is more suitable for detecting intra-membrane Aβ oligomers and extra-membrane Aβ oligomers states. As such, our findings provide an efficient method for analyzing Aβ proteins or other proteins that are easily aggregated in solution and in phospholipid membranes.</description><subject>Alzheimer Disease - etiology</subject><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer's disease</subject><subject>Alzheimers disease</subject><subject>Amyloid beta-Peptides - chemistry</subject><subject>Amyloid beta-Peptides - ultrastructure</subject><subject>Biology and Life Sciences</subject><subject>Cross-Linking Reagents</subject><subject>Crosslinking</subject><subject>Dementia</subject><subject>Detergents</subject><subject>Electrophoresis</subject><subject>Epidermal growth factor</subject><subject>Experimental methods</subject><subject>Glutaral</subject><subject>Glutaraldehyde</subject><subject>Humans</subject><subject>Ligands</subject><subject>Medicine and Health Sciences</subject><subject>Membranes</subject><subject>Membranes, Artificial</subject><subject>Microscopy</subject><subject>Microscopy, Electron, Transmission</subject><subject>Oligomers</subject><subject>Pathogenesis</subject><subject>Peptide Fragments - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shi, Jing-Ming</au><au>Pei, Jie</au><au>Liu, En-Qi</au><au>Zhang, Lin</au><au>Subramanyam, Rajagopal</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bis(sulfosuccinimidyl) suberate (BS3) crosslinking analysis of the behavior of amyloid-β peptide in solution and in phospholipid membranes</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2017-03-21</date><risdate>2017</risdate><volume>12</volume><issue>3</issue><spage>e0173871</spage><epage>e0173871</epage><pages>e0173871-e0173871</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The structure and state of amyloid-β peptide (Aβ) oligomers often need to be checked by reliable experimental methods. Electrophoresis is a commonly applied measurement method. However, due to the presence of detergents, oligomers are easily broken during electrophoresis, which makes it very hard to accurately assess Aβ aggregate states. In the current study, bis(sulfosuccinimidyl) suberate (BS3) was used to cross-link Aβ1-42 oligomers prior to electrophoresis. When compared to a previously reported Aβ cross-linking agent, glutaraldehyde, it was quite apparent that BS3 is more suitable for detecting intra-membrane Aβ oligomers and extra-membrane Aβ oligomers states. As such, our findings provide an efficient method for analyzing Aβ proteins or other proteins that are easily aggregated in solution and in phospholipid membranes.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>28323849</pmid><doi>10.1371/journal.pone.0173871</doi><orcidid>https://orcid.org/0000-0002-8185-3130</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Alzheimer Disease - etiology Alzheimer Disease - metabolism Alzheimer's disease Alzheimers disease Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - ultrastructure Biology and Life Sciences Cross-Linking Reagents Crosslinking Dementia Detergents Electrophoresis Epidermal growth factor Experimental methods Glutaral Glutaraldehyde Humans Ligands Medicine and Health Sciences Membranes Membranes, Artificial Microscopy Microscopy, Electron, Transmission Oligomers Pathogenesis Peptide Fragments - chemistry Peptide Fragments - ultrastructure Peptides Phospholipids Physical Sciences Protein Aggregates Protein Aggregation, Pathological - etiology Protein Aggregation, Pathological - metabolism Proteins Research and Analysis Methods Solutions Succinimides Toxicity β-Amyloid |
| title | Bis(sulfosuccinimidyl) suberate (BS3) crosslinking analysis of the behavior of amyloid-β peptide in solution and in phospholipid membranes |
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