Salt Modulated Fibrillar Aggregation of the Sweet Protein MNEI in Aqueous Solution

Salt Modulated Fibrillar Aggregation of the Sweet Protein MNEI in Aqueous Solution The mechanism of conversion of globular native proteins into amyloid fibrils represents one of the most attractive research topics in biophysics, because of its involvement in the development of severe pathologies and in various biotechnological processes. Aqueous medium properties, such as pH and ionic strength, as well as interactions with other species in solution, play a key role in tuning the fibrillization process. Here, we describe a comparative study of the influence of different ions from the Hofmeister series on the thermal unfolding and aggregation propensity of MNEI, a model protein, selected because of its tendency to form amyloid aggregates at acidic pH, even at temperatures well below its melting temperature. By selecting a temperature at which only negligible amounts of protein are unfolded, we have focused on the effect of ions on fibril formation. ThT fluorescence experiments indicated that all the salts examined increased the rate and the extent of fibrillization. Moreover, we found that anions, particularly sulfate, strongly influence the process, which instead is only marginally affected by different cations. Finally, a specific link to the chloride concentration was detected. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Solution Chemistry Springer Journals

Salt Modulated Fibrillar Aggregation of the Sweet Protein MNEI in Aqueous Solution

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Publisher
Springer Journals
Copyright
Copyright © 2018 by Springer Science+Business Media, LLC, part of Springer Nature
Subject
Chemistry; Physical Chemistry; Industrial Chemistry/Chemical Engineering; Geochemistry; Oceanography; Inorganic Chemistry; Condensed Matter Physics
ISSN
0095-9782
eISSN
1572-8927
D.O.I.
10.1007/s10953-018-0764-6
Publisher site
See Article on Publisher Site

Abstract

The mechanism of conversion of globular native proteins into amyloid fibrils represents one of the most attractive research topics in biophysics, because of its involvement in the development of severe pathologies and in various biotechnological processes. Aqueous medium properties, such as pH and ionic strength, as well as interactions with other species in solution, play a key role in tuning the fibrillization process. Here, we describe a comparative study of the influence of different ions from the Hofmeister series on the thermal unfolding and aggregation propensity of MNEI, a model protein, selected because of its tendency to form amyloid aggregates at acidic pH, even at temperatures well below its melting temperature. By selecting a temperature at which only negligible amounts of protein are unfolded, we have focused on the effect of ions on fibril formation. ThT fluorescence experiments indicated that all the salts examined increased the rate and the extent of fibrillization. Moreover, we found that anions, particularly sulfate, strongly influence the process, which instead is only marginally affected by different cations. Finally, a specific link to the chloride concentration was detected.

Journal

Journal of Solution ChemistrySpringer Journals

Published: May 17, 2018

References

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