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Das, Anuj Kumer, 2012. Proteomics studies of neurotoxic amyloid β oligomers using size exclusion chromatography. Second cycle, A2E. Uppsala: SLU, Dept. of Molecular Biology (until 131231)



The prime toxic species that causes Alzheimer’s disease is believed to be oligomeric aggregates of the amyloid β peptide (Aβ). The major aim of the work was to develop methods to study which proteins in human plasma that interacts with oligomeric neurotoxic forms of Aβ. The interactions of Aβ with human biological fluid proteins are important for drug discovery efforts against Alzheimer’s disease but still not very well explored. Stable peptide oligomers were formed by a special variant of Aβ (called Aβ42cc). The co-elution of Aβ42cc oligomers with human blood serum was carried out using size exclusion chromatography (SEC). The eluted fractions were analyzed by SDS-PAGE but no strong interaction between Aβ oligomers and blood serum proteins could be observe.

Main title:Proteomics studies of neurotoxic amyloid β oligomers using size exclusion chromatography
Authors:Das, Anuj Kumer
Supervisor:Lendel, Christofer
Examiner:Ståhlberg, Jerry
Volume/Sequential designation:UNSPECIFIED
Year of Publication:2012
Level and depth descriptor:Second cycle, A2E
Student's programme affiliation:NM003 Biotechnology - Master's Programme 120 HEC
Supervising department:(NL, NJ) > Dept. of Molecular Biology (until 131231)
Keywords:Alzheimer’s disease, proteomics, amyloid-β oligomers, size exclusion chromatography
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Subject. Use of subject categories until 2023-04-30.:Life sciences
Deposited On:28 Nov 2012 12:03
Metadata Last Modified:28 Nov 2012 12:03

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