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The effect of protein chaperones HspB6 and the monomeric form of the protein 14-3-3ζ (14-3-3ζ m ) on a test system based on thermal aggregation of UV-irradiated glycogen phosphorylase b (UV-Ph b ) at 37 °C and a constant ionic strength (0.15 M) was studied using dynamic light scattering. A significant increase in the anti-aggregation activity of HspB6 and 14-3-3ζ m was demonstrated in the presence of 0.1 M arginine (Arg). To compare the effects of these chaperones on UV-Ph b aggregation, the values of initial stoichiometry of the chaperone-target protein complex ( S  0 ) were used. The analysis of the S  0 values shows that in the presence of Arg fewer chaperone subunits are needed to completely prevent aggregation of the UV-Ph b subunit. The changes in the structures of HspB6 and 14-3-3ζ m induced by binding of Arg were evaluated by the fluorescence spectroscopy and differential scanning calorimetry. It was suggested that Arg caused conformational changes in chaperone molecules, which led to a decrease in the thermal stability of protein chaperones and their destabilization.

Effect of Arginine on Chaperone-Like Activity of HspB6 and Monomeric 14-3-3ζ