Assessment of the Aggregation Propensity of the beta-amyloid Peptide During the Synthesis and when Free in Solution

Assessment of the Aggregation Propensity of the beta-amyloid Peptide During the Synthesis and when Free in Solution

Author Malavolta, Luciana Autor UNIFESP Google Scholar
Pinto, Marcelo Rodrigo Silva Autor UNIFESP Google Scholar
Nakaie, Clovis Ryuichi Autor UNIFESP Google Scholar
Institution Fac Ciencias Med Santa Casa Sao Paulo
Universidade Federal de São Paulo (UNIFESP)
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.
Keywords beta-amyloid peptide
electron spin resonance
fibril formation
peptide solubilization
polymer
polymer solvation
Language English
Sponsor Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
FADA
Date 2013-08-01
Published in Protein And Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 20, n. 8, p. 848-855, 2013.
ISSN 0929-8665 (Sherpa/Romeo, impact factor)
Publisher Bentham Science Publ Ltd
Extent 848-855
Origin http://dx.doi.org/10.2174/0929866511320080002
Access rights Closed access
Type Article
Web of Science ID WOS:000320305100002
URI http://repositorio.unifesp.br/11600/45150

Show full item record




File

File Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Search


Browse

Statistics

My Account