Biomimetic nuclear lamin fibers with remarkable toughness and stiffness

Maayan Khayat, Shani Deri, David Wolf, Tom Trigano, Ohad Medalia, Kfir Ben-Harush

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


The native hagfish slime threads, which are made up of two intermediate filament (IF)-like proteins, exhibit mechanical properties comparable to dragline spider silk fiber, the toughest fiber in nature. However, unlike silk, the design of artificial IF-protein-based fibers has been rarely studied, possibly because the unique hierarchical organization of the keratin-like proteins within these threads is challenging to mimic, and consequently, extraordinary fiber mechanics has not been shown in slime threads from recombinant IF-protein-based system. Here, we have reported the synthesis and properties of recombinant type V IF-protein, based on the Caenorhabditis elegans (Ce) lamin gene. The protein was solubilized and wet-spun into aqueous solutions to prepare Ce-lamin fibers by varying injection flow rates and Ca+2 ion concentrations in the coagulation buffer. At specific set of conditions, Ce-lamin fibers demonstrated remarkable toughness and stiffness, comparable to hagfish slime threads and natural dragline spider silk. Transmission electron microscopy analysis showed that paracrystals were the main nanometric structure within the fibers. This study demonstrates that outstanding mechanical properties can be achieved with recombinant IF-proteins through self-organization. Thus, these results have broadened the pool of fibrous proteins that can be used in functional materials for a diverse range of applications.

Original languageEnglish
Pages (from-to)2060-2067
Number of pages8
JournalInternational Journal of Biological Macromolecules
StatePublished - 15 Nov 2020


  • Biomimetic fiber
  • Intermediate filaments
  • Nuclear lamin
  • Protein self-assembly
  • Toughness


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