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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

Author(s): Luciana Malavolta, Marcelo R.S. Pinto and Clóvis R. Nakaie

Volume 20, Issue 8, 2013

Page: [848 - 855] Pages: 8

DOI: 10.2174/0929866511320080002

Price: $65

Abstract

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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