Disulfide-linked Foldon Domains To Stabilize Protein Trimers

Researchers in Dr. James Swartz's lab have developed foldon domains that can be used to stabilize protein trimers even under stressful conditions that would otherwise disassemble the trimeric structure. The ability to trimerize proteins is of great interest for biomaterial applications, such as vaccine development. Proteins such as influenza hemagglutinin naturally form trimeric structures. When used as vaccines, such trimers may disassemble before the vaccine can be administered. This technology overcomes this limitation by providing stable covalent bonds between the monomers of trimeric protein structures without affecting the conformation of the trimeric protein.

Stage of Research
The inventors have optimized the foldon monomer and folding conditions. In addition, when used with a hemagglutinin stem domain protein the correct immunogenic conformation of this stabilized HA stem trimer was obtained and confirmed.