Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 16, Issue 3, Pages 885-889Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3cp54151g
Keywords
-
Funding
- Department of Biotechnology [BT/53/NE/TBP/2010]
- Faculty to faculty collaboration'' grant from ARCI [ARCI/D/FAO/Nano/K-16/Canada/11]
Ask authors/readers for more resources
Decoupling conformational changes from aggregation will help us understand amyloids better. Here we attach Alzheimer's amyloid-beta(1-40) monomers to silver nanoparticles, preventing their aggregation, and study their conformation under aggregation-favoring conditions using SERS. Surprisingly, the alpha-helical character of the peptide remains unchanged between pH 10.5 and 5.5, while the solubility changes >100X. Amyloid aggregation can therefore start without significant conformational changes.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available