Jump to main content
Jump to site search

Issue 3, 2014
Previous Article Next Article

pH changes the aggregation propensity of amyloid-β without altering the monomer conformation

Author affiliations

Abstract

Decoupling conformational changes from aggregation will help us understand amyloids better. Here we attach Alzheimer's amyloid-β1–40 monomers to silver nanoparticles, preventing their aggregation, and study their conformation under aggregation-favoring conditions using SERS. Surprisingly, the α-helical character of the peptide remains unchanged between pH 10.5 and 5.5, while the solubility changes >100×. Amyloid aggregation can therefore start without significant conformational changes.

Graphical abstract: pH changes the aggregation propensity of amyloid-β without altering the monomer conformation

Back to tab navigation

Supplementary files

Publication details

The article was received on 01 Oct 2013, accepted on 05 Nov 2013 and first published on 05 Nov 2013


Article type: Communication
DOI: 10.1039/C3CP54151G
Citation: Phys. Chem. Chem. Phys., 2014,16, 885-889
  •   Request permissions

    pH changes the aggregation propensity of amyloid-β without altering the monomer conformation

    D. Bhowmik, C. M. MacLaughlin, M. Chandrakesan, P. Ramesh, R. Venkatramani, G. C. Walker and S. Maiti, Phys. Chem. Chem. Phys., 2014, 16, 885
    DOI: 10.1039/C3CP54151G

Search articles by author

Spotlight

Advertisements