Fig 1.
Transmission electron microscopic (TEM) images of (A) insulin and (B) lysozyme fibrils after 36 h of incubation.
Fig 2.
Chemical structures of osmolytes (A) proline and (B) sorbitol.
Fig 3.
Kinetics of insulin (A) and (B) and lysozyme (C) and (D) fibril extension in absence and presence of different concentration of proline and sorbitol respectively.
Table 1.
Fibrillation kinetics parameter for Insulin and lysozyme.
Fig 4.
TEM images of insulin (A) and (B) in presence of 100 mM proline and sorbitol respectively and lysozyme (C) and (D) in presence of 500 mM proline and sorbitol respectively.
Fig 5.
Kinetics of (A) insulin and (B) lysozyme fibrillation monitored by the binding of ThT with amyloid fibrils in presence of proline, sorbitol and their mixture, and TEM images of (C) insulin and (D) lysozyme in presence of mixture of proline and sorbitol.
Fig 6.
Enthalpies of interaction of insulin in presence of 100 mM proline, sorbitol and their mixture at (A) native, (B) elongation and (C) saturation stages of fibrillation.
Fig 7.
Comparison between sum of the enthalpies of interaction of insulin in presence of 100 mM proline and sorbitol individually and in their mixture at (A) native, (B) elongation and (C) saturation stages of fibrillation.
Fig 8.
The sum of limiting standard enthalpies of interaction of insulin in 100 mM proline and sorbitol individually and in the mixture of osmolytes at different stages of fibrillation.
Table 2.
The limiting standard enthalpies of interaction ().