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Effects of Trehalose on Thermodynamic Properties of Alpha-synuclein Revealed through Synchrotron Radiation Circular Dichroism.

Ruzza P, Hussain R, Biondi B, Calderan A, Tessari I, Bubacco L, Siligardi G - Biomolecules (2015)

Bottom Line: Many neurodegenerative diseases, including Huntington's, Alzheimer's and Parkinson's diseases, are characterized by protein misfolding and aggregation.Our study indicated that a low trehalose concentration stabilized α-synuclein folding much better than at high concentration by blocking in vitro α-synuclein's polymerisation.These results suggested that trehalose could be associated with other drugs leading to a new approach for treating Parkinson's and other brain-related diseases.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biomolecular Chemistry of CNR, Padua Unit, Padua 35131, Italy. paolo.ruzza@cnr.it.

ABSTRACT
Many neurodegenerative diseases, including Huntington's, Alzheimer's and Parkinson's diseases, are characterized by protein misfolding and aggregation. The capability of trehalose to interfere with protein misfolding and aggregation has been recently evaluated by several research groups. In the present work, we studied, by means of synchrotron radiation circular dichroism (SRCD) spectroscopy, the dose-effect of trehalose on α-synuclein conformation and/or stability to probe the capability of this osmolyte to interfere with α-synuclein's aggregation. Our study indicated that a low trehalose concentration stabilized α-synuclein folding much better than at high concentration by blocking in vitro α-synuclein's polymerisation. These results suggested that trehalose could be associated with other drugs leading to a new approach for treating Parkinson's and other brain-related diseases.

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Far-UV synchrotron radiation circular dichroism (SRCD) spectra of α-synuclein alone or in presence of 10 or 100 mM trehalose. α-Synuclein concentration was 0.36 mg/mL in PBS buffer, pH 7.4.
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biomolecules-05-00724-f002: Far-UV synchrotron radiation circular dichroism (SRCD) spectra of α-synuclein alone or in presence of 10 or 100 mM trehalose. α-Synuclein concentration was 0.36 mg/mL in PBS buffer, pH 7.4.

Mentions: The CD spectrum of α-synuclein showed a negative CD band at about 197 nm characteristic of the disordered structure in aqueous environment (Figure 2). The CD intensity at 197 nm was not affected by the presence of trehalose at low concentration (10 mM), but marginally at higher concentration of 100 mM (Figure 2).


Effects of Trehalose on Thermodynamic Properties of Alpha-synuclein Revealed through Synchrotron Radiation Circular Dichroism.

Ruzza P, Hussain R, Biondi B, Calderan A, Tessari I, Bubacco L, Siligardi G - Biomolecules (2015)

Far-UV synchrotron radiation circular dichroism (SRCD) spectra of α-synuclein alone or in presence of 10 or 100 mM trehalose. α-Synuclein concentration was 0.36 mg/mL in PBS buffer, pH 7.4.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4496693&req=5

biomolecules-05-00724-f002: Far-UV synchrotron radiation circular dichroism (SRCD) spectra of α-synuclein alone or in presence of 10 or 100 mM trehalose. α-Synuclein concentration was 0.36 mg/mL in PBS buffer, pH 7.4.
Mentions: The CD spectrum of α-synuclein showed a negative CD band at about 197 nm characteristic of the disordered structure in aqueous environment (Figure 2). The CD intensity at 197 nm was not affected by the presence of trehalose at low concentration (10 mM), but marginally at higher concentration of 100 mM (Figure 2).

Bottom Line: Many neurodegenerative diseases, including Huntington's, Alzheimer's and Parkinson's diseases, are characterized by protein misfolding and aggregation.Our study indicated that a low trehalose concentration stabilized α-synuclein folding much better than at high concentration by blocking in vitro α-synuclein's polymerisation.These results suggested that trehalose could be associated with other drugs leading to a new approach for treating Parkinson's and other brain-related diseases.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biomolecular Chemistry of CNR, Padua Unit, Padua 35131, Italy. paolo.ruzza@cnr.it.

ABSTRACT
Many neurodegenerative diseases, including Huntington's, Alzheimer's and Parkinson's diseases, are characterized by protein misfolding and aggregation. The capability of trehalose to interfere with protein misfolding and aggregation has been recently evaluated by several research groups. In the present work, we studied, by means of synchrotron radiation circular dichroism (SRCD) spectroscopy, the dose-effect of trehalose on α-synuclein conformation and/or stability to probe the capability of this osmolyte to interfere with α-synuclein's aggregation. Our study indicated that a low trehalose concentration stabilized α-synuclein folding much better than at high concentration by blocking in vitro α-synuclein's polymerisation. These results suggested that trehalose could be associated with other drugs leading to a new approach for treating Parkinson's and other brain-related diseases.

Show MeSH
Related in: MedlinePlus