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Int J Mass Spectrom. 2011 Apr 30;302(1-3):167-173.

Hydrogen exchange mass spectrometry as an analytical tool for the analysis of amyloid fibrillogenesis.

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1
Center for Insoluble Protein Structure and Interdisciplinary Nanoscience Center (iNANO) at the Department of Molecular Biology, Science Park, University of Aarhus, Gustav Wieds Vej 10c, 8000 Aarhus C, Denmark.

Abstract

In this study, we have used glucagon as a model system for analyzing amyloid fibrillogenesis by hydrogen exchange MALDI mass spectrometry (HXMS). The hydrogen exchange mass spectrometry data correlated well with the traditional method based on Thioflavin T fluorescence and provided quantitative information by measuring the fibrillating molecules directly. The hydrogen exchange mass spectrometry data collected during fibrillogenesis revealed that glucagon fibrillation was a two component system showing an on/off type of interaction where only monomeric and fibrils were present without any substantial amount of intermediate species. This was evident by the extensive deuteration of the monomer and protection of the entire 29 residue glucagon peptide upon fibrillation.. The method complements the traditional procedures and has the potential to provide new information with respect to the nature of transient species, the structure of the growing fibrils and the mechanism of formation.

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