There is considerable interest in protein therapeutics and proteins as chemical and biochemical reagents. However, proteins are unstable to outside stressors such as heat, pH changes, and desiccation. We synthesized three trehalose monomer regioisomers using Williamson etherification. Each monomer regioisomer was modified with a styrenyl ether moiety at either the O2, O4, or O6 position on trehalose. Four polymers were synthesized via reversible addition-fragmentation chain transfer (RAFT) polymerization, three polymers employing each regioisomer separately and one polymer incorporating all regioisomers. We then compared their protein stabilization capabilities to heat stress using the model protein lysozyme to observe any changes in stabilization caused by differences in conformation from the different modification sites.

Study on the effect of modification site on the trehalose polymers on protein stabilization

251st National Meeting (2016)

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