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Trehalose Effect on The Aggregation of Model Proteins into Amyloid Fibrils

1
Department of Life and Environmental Sciences, Polytechnic University of Marche, I-60121 Ancona, Italy
2
Department of Chemistry “Giacomo Ciamician”, University of Bologna, I-40126 Bologna, Italy
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Life 2020, 10(5), 60; https://doi.org/10.3390/life10050060
Received: 31 March 2020 / Revised: 7 May 2020 / Accepted: 8 May 2020 / Published: 13 May 2020
(This article belongs to the Section Biochemistry, Biophysics and Computational Biology)
Protein aggregation into amyloid fibrils is a phenomenon that attracts attention from a wide and composite part of the scientific community. Indeed, the presence of mature fibrils is associated with several neurodegenerative diseases, and in addition these supramolecular aggregates are considered promising self-assembling nanomaterials. In this framework, investigation on the effect of cosolutes on protein propensity to aggregate into fibrils is receiving growing interest, and new insights on this aspect might represent valuable steps towards comprehension of highly complex biological processes. In this work we studied the influence exerted by the osmolyte trehalose on fibrillation of two model proteins, that is, lysozyme and insulin, investigated during concomitant variation of the solution ionic strength due to NaCl. In order to monitor both secondary structures and the overall tridimensional conformations, we have performed UV spectroscopy measurements with Congo Red, Circular Dichroism, and synchrotron Small Angle X-ray Scattering. For both proteins we describe the effect of trehalose in changing the fibrillation pattern and, as main result, we observe that ionic strength in solution is a key factor in determining trehalose efficiency in slowing down or blocking protein fibrillation. Ionic strength reveals to be a competitive element with respect to trehalose, being able to counteract its inhibiting effects toward amyloidogenesis. Reported data highlight the importance of combining studies carried out on cosolutes with valuation of other physiological parameters that may affect the aggregation process. Also, the obtained experimental results allow to hypothesize a plausible mechanism adopted by the osmolyte to preserve protein surface and prevent protein fibrillation. View Full-Text
Keywords: small angle X-ray scattering; circular dichroism; spectroscopy; amyloid; trehalose; protein solvation; lysozyme; insulin small angle X-ray scattering; circular dichroism; spectroscopy; amyloid; trehalose; protein solvation; lysozyme; insulin
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MDPI and ACS Style

Mari, E.; Ricci, C.; Pieraccini, S.; Spinozzi, F.; Mariani, P.; Ortore, M.G. Trehalose Effect on The Aggregation of Model Proteins into Amyloid Fibrils. Life 2020, 10, 60. https://doi.org/10.3390/life10050060

AMA Style

Mari E, Ricci C, Pieraccini S, Spinozzi F, Mariani P, Ortore MG. Trehalose Effect on The Aggregation of Model Proteins into Amyloid Fibrils. Life. 2020; 10(5):60. https://doi.org/10.3390/life10050060

Chicago/Turabian Style

Mari, Eleonora; Ricci, Caterina; Pieraccini, Silvia; Spinozzi, Francesco; Mariani, Paolo; Ortore, Maria G. 2020. "Trehalose Effect on The Aggregation of Model Proteins into Amyloid Fibrils" Life 10, no. 5: 60. https://doi.org/10.3390/life10050060

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