Recombinant Silk Fibroin Crystalline Regions as Biomaterial Alternatives to the Full-Length Protein

Zifan Wang, Bogdan A. Serban, Monica A. Serban

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Silk fibroin is a natural polymer with a unique repetitive structure that translates to extraordinary properties in terms of processability and mechanical properties. The Bombyx mori silk has a molecular weight of ∼415 kDa and consists of a light chain and a heavy chain. Its heavy chain is organized into 12 crystalline domains. Each of these crystalline domains contains subdomains of ∼70 amino acid containing blocks. It is well understood that the heavy chain of the protein is responsible for its processing versatility and excellent mechanical properties; however, the need for the high number of monomeric repeating units is unclear, and the individual properties of crystalline regions compared to those of the full-length protein are not understood. The work described herein assessed the possibility of using recombinant crystalline regions as alternative biomaterials for applications such as tissue adhesives. Our results indicate that while the two tested substructures do not fully recapitulate the native silk fibroin's properties, they appear to be a suitable alternative for the production of silk-based medical adhesives.

Original languageEnglish
Pages (from-to)7004-7010
Number of pages7
JournalACS Biomaterials Science and Engineering
Issue number12
StatePublished - Dec 14 2020


  • protein interactions
  • recombinant expression
  • silk fibroin
  • structural changes


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