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Bis(sulfosuccinimidyl) suberate (BS3) crosslinking analysis of the behavior of amyloid-β peptide in solution and in phospholipid membranes
Author(s) -
JingMing Shi,
Jie Pei,
Enqi Liu,
Lin Zhang
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0173871
Subject(s) - phospholipid , membrane , peptide , biophysics , chemistry , amyloid (mycology) , biochemistry , biology , inorganic chemistry
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 (BS 3 ) 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 BS 3 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.

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