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Updated: May 5, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
pH changes the aggregation propensity of amyloid-β without altering the monomer conformation
Debanjan Bhowmik1, Christina M MacLaughlin, Muralidharan Chandrakesan
1Department of Chemistry, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai 400005, India. maiti@tifr.res.in.
Abstract:
Decoupling conformational changes from aggregation will help us understand amyloids better. Here we attach Alzheimer's amyloid-β(1-40) 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.
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