Design of a Redox-Sensitive Supramolecular Protein Assembly System Operating in Live Cells

Giuliano Bellapadrona, Michael Elbaum

Research output: Contribution to journalArticlepeer-review


A fusion construct between Citrine (a YFP variant) and human ferritin (H-chain) was recently shown to form supramolecular assemblies of micrometer size when expressed in mammalian cells. The assembly process is driven by weak hydrophobic interactions leading to dimerization of YFP. Protein assembly could be suppressed at the gene level by mutation in the primary sequence of the construct. In this work, we describe the engineering of a self-assembly interface sensitive to redox state in the cell. Key hydrophobic residues of YFP were mutated systematically to cysteines. Supramolecular assembly of the Citrine-ferritin construct was in some cases preserved by formation of disulfide bonds in place of hydrophobic interactions. In others cases, assembly was abolished, resulting in a diffuse distribution of the expressed protein. A specific variant that remained diffuse under normally reducing intracellular conditions was found to self-assemble rapidly upon exposure to a thiol-specific oxidizing reagent.

Original languageEnglish
Pages (from-to)6231-6235
Number of pages5
JournalNano Letters
Issue number10
StatePublished - 12 Oct 2016

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • Condensed Matter Physics
  • Mechanical Engineering
  • Bioengineering
  • General Materials Science


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