title: pH changes the aggregation propensity of amyloid-β without altering the monomer conformation.
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.
authors.affiliation: Department of Chemistry, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai 400005, India. maiti@tifr.res.in.
authors.forename: Debanjan
authors.initials: D
authors.lastname: Bhowmik
authors.forename: Christina M
authors.initials: CM
authors.lastname: MacLaughlin
authors.forename: Muralidharan
authors.initials: M
authors.lastname: Chandrakesan
authors.forename: Prashanth
authors.initials: P
authors.lastname: Ramesh
authors.forename: Ravindra
authors.initials: R
authors.lastname: Venkatramani
authors.forename: Gilbert C
authors.initials: GC
authors.lastname: Walker
authors.forename: Sudipta
authors.initials: S
authors.lastname: Maiti
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D053768:Metal Nanoparticles / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D012834:Silver / Q000737:chemistry
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); D012834:Silver