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Issue 3, 2014
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pH changes the aggregation propensity of amyloid-β without altering the monomer conformation

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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

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Article information


Submitted
01 Oct 2013
Accepted
05 Nov 2013
First published
05 Nov 2013

Phys. Chem. Chem. Phys., 2014,16, 885-889
Article type
Communication

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

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