This work developed an alternative approach targeting the evaluation of the aggregation propensity of the (1-
42) β-amyloid peptide (Alzheimer’s disease) and some segments, either attached to a polymer during their synthesis or
when free in solution. The solvation behavior of peptide-resins was gauged by measuring the swelling of beads in a microscope
and the degree of chain motion through EPR spectra of previously labeled resins with an amino acid-type probe.
In terms of comparative solvent dissociation power towards aggregated structures, the findings revealed greater values of
peptide-resin swelling, peptide chain mobility and solubility when in strong electron donor dimethylsulfoxide than in
strong electron acceptor trifluoroethanol. Otherwise, the weakest chain-chain disruption power was verified for acetonitrile,
an internally neutral solvent in terms of Lewis acid/base properties. In complement, fluorescence and light scattering
experiments depicted that the 15-35 region plays an essential role in the amyloid peptide fibril formation capacity.
Keywords: β-amyloid peptide, electron spin resonance, fibril formation, peptide solubilization, polymer, polymer solvation.
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