Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/45150
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)
Keywords: beta-amyloid peptide
electron spin resonance
fibril formation
peptide solubilization
polymer
polymer solvation
Issue Date: 1-Aug-2013
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.
URI: http://repositorio.unifesp.br/11600/45150
ISSN: 0929-8665
Other Identifiers: http://dx.doi.org/10.2174/0929866511320080002
Appears in Collections:Artigo

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