Details

Autor(en) / Beteiligte

• Eronina, Tatiana B.
• Mikhaylova, Valeriya V.
• Chebotareva, Natalia A.
• Shubin, Vladimir V.
• Sluchanko, Nikolai N.
• Kurganov, Boris I.

Titel

Comparative effects of trehalose and 2-hydroxypropyl-β-cyclodextrin on aggregation of UV-irradiated muscle glycogen phosphorylase b

Ist Teil von

• Biochimie, 2019-10, Vol.165, p.196-205

Ort / Verlag

France: Elsevier B.V

Erscheinungsjahr

2019

Quelle

MEDLINE

Beschreibungen/Notizen

• Chemical chaperones are a class of small molecules which enhance folding and prevent aggregation of proteins. Investigation of their effects on the processes of protein aggregation is of importance for further understanding of implication of protein aggregation in neurodegenerative diseases, as well as for solving biotechnological tasks. The effects of chemical chaperones trehalose and 2-hydroxypropyl-β-cyclodextrin (HP-β-CD) on the kinetics of aggregation of UV-irradiated muscle glycogen phosphorylase b (UV-Phb) at 37 °C have been studied. The process of thermal aggregation of UV-Phb includes a slow stage of structural reorganization of the UV-Phb molecule, nucleation stage and fast attachment of structurally reorganized UV-Phb molecules to nuclei formed during the nucleation stage. It was shown that both trehalose and HP-β-CD increased the duration of the nucleation phase and slowed down the rate of structural reorganization of the UV-Phb molecule. This conclusion has been confirmed by the circular dichroism data. In the absence of chaperones, 82% UV-Phb aggregates, whereas in the presence of HP-β-CD or trehalose the portion of aggregated protein decreases to 70 and 66%, respectively. The data on analytical ultracentrifugation demonstrated that in the presence of these additives the size of protein aggregates decreased. Analysis of the combined effect of trehalose and HP-β-CD on UV-Phb aggregation showed that protein aggregation was independently affected by trehalose and HP-β-CD. •Trehalose and 2-hydroxypropyl-β-cyclodextrin are tested as chemical chaperones.•Anti-aggregation activity of chemical chaperones was quantitatively characterized.•UV-irradiated glycogen phosphorylase b (UV-Phb) was used as a target protein.•Chemical chaperones retard structural reorganization of UV-Phb.•Extension of nucleation stage was observed in the presence of chemical chaperones.