Sweet stability
Licentiatavhandling, 2024
In this thesis, the stabilising effect of trehalose is compared with that of sucrose, a structurally similar disaccharide. This comparison aims to solve unanswered questions regarding their interactions with proteins and surrounding water molecules. X-ray and neutron scattering confirmed that myoglobin is preferentially hydrated by water and revealed that trehalose slows down the dynamics of the protein to a greater extent than sucrose, with minimal direct interaction. Differential scanning calorimetry showed that both disaccharides increase the denaturation temperature of the protein lysozyme, sucrose slightly more than trehalose. Additionally, the glass transition temperature of trehalose is marginally higher. Small and wide-angle x-ray scattering demonstrated that both sugars inhibit amyloid fibril formation.
The findings suggest that the effectiveness of both disaccharides in stabilising proteins varies with temperature; trehalose is more effective at lower temperatures around the glass transition, whereas sucrose may be slightly more efficient at higher temperatures around protein denaturation.
myoglobin
lysozyme
amyloid fibrils
DSC
trehalose
protein denaturation
neutron scattering
glass transition
sucrose
Författare
Kajsa Ahlgren
Chalmers, Fysik, Nano- och biofysik
Ämneskategorier
Fysik
Utgivare
Chalmers
PJ
Opponent: Margaret Holme