Title: Comparison of ¹H-NMR spectra by normalisation algorithms for studying amyloid toxicity in cells

Authors: Rocco Romano; Silvia Vilasi; Fausto Acernese; Rosangela Canonico; Annalisa Vilasi; Gerardo Giordano; Fabrizio Barone

Addresses: Department of Pharmacy, Università degli Studi di Salerno, Via Giovanni Paolo II, 128, I-84084 - Fisciano (SA), Italy ' Institute of Biophysics, National Research Council, Palermo, Italy ' Department of Pharmacy, Università degli Studi di Salerno, Via Giovanni Paolo II, 128, I-84084 - Fisciano (SA), Italy ' Dipartimento di Medicina e Chirurgia, Università degli Studi di Salerno, Via Salvator Allende, I-84081 Baronissi (SA), Italy ' Institute of Protein Biochemistry, National Research Council, Napoli, Italy ' Department of Pharmacy, Università degli Studi di Salerno, Via Giovanni Paolo II, 128, I-84084 - Fisciano (SA), Italy ' Dipartimento di Medicina e Chirurgia, Università degli Studi di Salerno, Via Salvator Allende, I-84081 Baronissi (SA), Italy

Abstract: A range of debilitating human diseases is associated with the formation of stable, highly organised, protein aggregates, the amyloid fibrils. Substantial evidence suggests that Prefibrillar Oligomeric Aggregates (PFAs), preceding mature fibrils formation, are the crucial species in the onset of the neuronal degeneration even if with mechanisms to be further cleared. In this work, we show how ¹H-NMR cell spectral analysis methods can prove to be very effective tools to clear the PFAs amyloid cytotoxicity mechanisms. Following the same method shown by Vilasi, we apply a new ¹H-NMR analysis algorithm to identify the metabolites significantly varied in cells incubated with toxic oligomers from the amyloidogenic W7FW14F mutant of apomyoglobin. Our main aim is to confirm the results obtained by Vilasi et al., normalising a set of different data spectra with the new PRICONA algorithm here described, thus contributing to strengthen the general framework of metabolites and proteins involved in cellular amyloid toxicity.

Keywords: amyloid fibrils; cellular amyloid toxicity; cells; biomedical engineering; amyloid cytotoxicity mechanisms; ¹H-NMR analysis; normalisation algorithm; protein aggregates; neuronal degeneration; metabolites; proteins.

DOI: 10.1504/IJBET.2013.058540

International Journal of Biomedical Engineering and Technology, 2013 Vol.13 No.4, pp.370 - 382

Received: 03 Dec 2012
Accepted: 07 Oct 2013
Published online: 27 Sep 2014 *

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