Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways
Brigham and Women's Hospital · Harvard University · +2 more institutions
Abstract
Amyloid β-protein (Aβ) is linked to neuronal injury and death in Alzheimer's disease (AD). Of particular relevance for elucidating the role of Aβ in AD is new evidence that oligomeric forms of Aβ are potent neurotoxins that play a major role in neurodegeneration and the strong association of the 42-residue form of Aβ, Aβ42, with the disease. Detailed knowledge of the structure and assembly dynamics of Aβ thus is important for the development of properly targeted AD therapeutics. Recently, we have shown that Aβ oligomers can be cross-linked efficiently, and their relative abundances quantified, by using the technique of photo-induced cross-linking of unmodified proteins (PICUP). Here, PICUP, size-exclusion…
Citation impact
- FWCI
- 14.14
- Percentile
- 100%
- References
- 40
Authors
6- GBGal Bitan
Brigham and Women's Hospital, Harvard University, Materials Processing (United States), Massachusetts Institute of Technology
- MKMarina Kirkitadze
Brigham and Women's Hospital, Harvard University, Materials Processing (United States), Massachusetts Institute of Technology
- ALAleksey Lomakin
Brigham and Women's Hospital, Harvard University, Materials Processing (United States), Massachusetts Institute of Technology
- SSSabrina S. Vollers
Brigham and Women's Hospital, Harvard University, Materials Processing (United States), Massachusetts Institute of Technology
- GBGeorge B. Benedek
Brigham and Women's Hospital, Harvard University, Materials Processing (United States), Massachusetts Institute of Technology
Topics & keywords
- Neurodegeneration
- Circular dichroism
- Biophysics
- Chemistry
- Amyloid (mycology)
- Protein aggregation
- Peptide
- Protein structure