mechanisms of action for trehalose (tre) anti-protein aggregation:
tre molecules can form a coating layer around the protein that efficiently competes with the protein to form hydrogen bonds with the water molecules trapped between the protein and tre, reducing the number of protein-solvent hydrogen bonds and the accompanying electrostatic solvation forces. A reduction in the solvation forces can consequently lead to an increase in intraprotein interactions, and a stabilization of the protein native structure.
key water molecules are thought to be replaced by sugar molecules which then provide the necessary interactions to stabilize protein folding and cellular functions.
key water molecules are trapped on the protein surface by a cage of sugar molecules forming a higher viscosity layer around the protein
formaldehyde, a crosslinking agent, readily reacts with thiol and amino groups, causing polymerization of proteins.
Can trehalose inhibit aggregation caused by formaldehyde?
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