Assessment of the aggregation propensity of the β-amyloid peptide during the synthesis and when free in solution

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. © 2013 bentham science publishers.