Characterizing and Controlling Nanoscale Self-Assembly of Suckerin-12

Jasmine M. Hershewe, William D. Wiseman, James E. Kath, Chelsea C. Buck, Maneesh K. Gupta, Patrick B. Dennis, Rajesh R. Naik, Michael C. Jewett*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Structural proteins such as "suckerins"present promising avenues for fabricating functional materials. Suckerins are a family of naturally occurring block copolymer-type proteins that comprise the sucker ring teeth of cephalopods and are known to self-assemble into supramolecular networks of nanoconfined β-sheets. Here, we report the characterization and controllable, nanoscale self-assembly of suckerin-12 (S12). We characterize the impacts of salt, pH, and protein concentration on S12 solubility, secondary structure, and self-assembly. In doing so, we identify conditions for fabricating â100 nm nanoassemblies (NAs) with narrow size distributions. Finally, by installing a noncanonical amino acid (ncAA) into S12, we demonstrate the assembly of NAs that are covalently conjugated with a hydrophobic fluorophore and the ability to change self-assembly and β-sheet content by PEGylation. This work presents new insights into the biochemistry of suckerin-12 and demonstrates how ncAAs can be used to expedite and fine-tune the design of protein materials.

Original languageEnglish (US)
Pages (from-to)3388-3399
Number of pages12
JournalACS synthetic biology
Issue number12
StatePublished - Dec 18 2020


  • bioinspired materials
  • noncanonical amino acids
  • protein characterization
  • protein nanomaterials
  • self-assembly
  • suckerins

ASJC Scopus subject areas

  • Biomedical Engineering
  • Biochemistry, Genetics and Molecular Biology (miscellaneous)


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