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|Title:||Assessment of the Aggregation Propensity of the beta-amyloid Peptide During the Synthesis and when Free in Solution|
|Authors:||Malavolta, Luciana [UNIFESP]|
Pinto, Marcelo Rodrigo Silva [UNIFESP]
Nakaie, Clovis Ryuichi [UNIFESP]
Fac Ciencias Med Santa Casa Sao Paulo
Universidade Federal de São Paulo (UNIFESP)
electron spin resonance
|Publisher:||Bentham Science Publ Ltd|
|Citation:||Protein And Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 20, n. 8, p. 848-855, 2013.|
|Abstract:||This work developed an alternative approach targeting the evaluation of the aggregation propensity of the (1-42) beta-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.|
|Appears in Collections:||Artigo|
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