Initial solvent conditions impact the reproducibility and aggregation trajectory of monomeric Amyloid Aβ

Our analysis indicates that solubilization with NaOH (50mM) offers a dependable method for solubilizing Aβ monomer. This results in monomeric and homogeneous peptide stock solutions, exhibiting exceptionally reproducible assembly kinetics when returned to near-neutral pH. Prior solubilization and monomerization of Aβ in HFIP, DMSO, AcN and NH4OH results in variable kinetics and extent of fibrillation. Prior exposure to these other solvents produces reproducible differences in aggregation even after monomerization in NaOH.